Enzyme Nomenclature

Continued from EC 1.9 to EC 1.12

EC 1.13

Acting on single donors with incorporation of molecular oxygen (oxygenases)

Sections

EC 1.13.11 With incorporation of two atoms of oxygen
EC 1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases)
EC 1.13.99 Miscellaneous


EC 1.13.11 with incorporation of two atoms of oxygen

Contents

EC 1.13.11.1 catechol 1,2-dioxygenase
EC 1.13.11.2 catechol 2,3-dioxygenase
EC 1.13.11.3 protocatechuate 3,4-dioxygenase
EC 1.13.11.4 gentisate 1,2-dioxygenase
EC 1.13.11.5 homogentisate 1,2-dioxygenase
EC 1.13.11.6 3-hydroxyanthranilate 3,4-dioxygenase
EC 1.13.11.7 deleted
EC 1.13.11.8 protocatechuate 4,5-dioxygenase
EC 1.13.11.9 2,5-dihydroxypyridine 5,6-dioxygenase
EC 1.13.11.10 7,8-dihydroxykynurenate 8,8a-dioxygenase
EC 1.13.11.11 tryptophan 2,3-dioxygenase
EC 1.13.11.12 linoleate 13S-lipoxygenase
EC 1.13.11.13 deleted
EC 1.13.11.14 2,3-dihydroxybenzoate 3,4-dioxygenase
EC 1.13.11.15 3,4-dihydroxyphenylacetate 2,3-dioxygenase
EC 1.13.11.16 3-carboxyethylcatechol 2,3-dioxygenase
EC 1.13.11.17 indole 2,3-dioxygenase
EC 1.13.11.18 sulfur dioxygenase
EC 1.13.11.19 cysteamine dioxygenase
EC 1.13.11.20 cysteine dioxygenase
EC 1.13.11.21 now EC 1.14.99.36
EC 1.13.11.22 caffeate 3,4-dioxygenase
EC 1.13.11.23 2,3-dihydroxyindole 2,3-dioxygenase
EC 1.13.11.24 quercetin 2,3-dioxygenase
EC 1.13.11.25 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase
EC 1.13.11.26 peptide-tryptophan 2,3-dioxygenase
EC 1.13.11.27 4-hydroxyphenylpyruvate dioxygenase
EC 1.13.11.28 2,3-dihydroxybenzoate 2,3-dioxygenase
EC 1.13.11.29 stizolobate synthase
EC 1.13.11.30 stizolobinate synthase
EC 1.13.11.31 arachidonate 12-lipoxygenase
EC 1.13.11.32 transferred now EC 1.13.12.16
EC 1.13.11.33 arachidonate 15-lipoxygenase
EC 1.13.11.34 arachidonate 5-lipoxygenase
EC 1.13.11.35 pyrogallol 1,2-oxygenase
EC 1.13.11.36 chloridazon-catechol dioxygenase
EC 1.13.11.37 hydroxyquinol 1,2-dioxygenase
EC 1.13.11.38 1-hydroxy-2-naphthoate 1,2-dioxygenase
EC 1.13.11.39 biphenyl-2,3-diol 1,2-dioxygenase
EC 1.13.11.40 arachidonate 8-lipoxygenase
EC 1.13.11.41 2,4'-dihydroxyacetophenone dioxygenase
EC 1.13.11.42 deleted
EC 1.13.11.43 lignostilbene αβ-dioxygenase
EC 1.13.11.44 deleted covered by EC 1.13.11.60 and EC 5.4.4.6
EC 1.13.11.45 linoleate 11-lipoxygenase
EC 1.13.11.46 4-hydroxymandelate synthase
EC 1.13.11.47 3-hydroxy-4-oxoquinoline 2,4-dioxygenase
EC 1.13.11.48 3-hydroxy-2-methyl-quinolin-4-one 2,4-dioxygenase
EC 1.13.11.49 chlorite O2-lyase
EC 1.13.11.50 acetylacetone-cleaving enzyme
EC 1.13.11.51 9-cis-epoxycarotenoid dioxygenase
EC 1.13.11.52 indoleamine 2,3-dioxygenase
EC 1.13.11.53 acireductone dioxygenase (Ni2+-requiring)
EC 1.13.11.54 acireductone dioxygenase [iron(II)-requiring]
EC 1.13.11.55 sulfur oxygenase/reductase
EC 1.13.11.56 1,2-dihydroxynaphthalene dioxygenase
EC 1.13.11.57 gallate dioxygenase
EC 1.13.11.58 linoleate 9S-lipoxygenase
EC 1.13.11.59 torulene dioxygenase
EC 1.13.11.60 linoleate 8R-lipoxygenase
EC 1.13.11.61 linolenate 9R-lipoxygenase
EC 1.13.11.62 linoleate 10R-lipoxygenase
EC 1.13.11.63 β-carotene 15,15'-dioxygenase
EC 1.13.11.64 5-nitrosalicylate dioxygenase
EC 1.13.11.65 carotenoid isomerooxygenase
EC 1.13.11.66 hydroquinone 1,2-dioxygenase
EC 1.13.11.67 8'-apo-β-carotenoid 14',13'-cleaving dioxygenase
EC 1.13.11.68 9-cis-β-carotene 9',10'-cleaving dioxygenase
EC 1.13.11.69 carlactone synthase
EC 1.13.11.70 all-trans-10'-apo-β-carotenal 13,14-cleaving dioxygenase
EC 1.13.11.71 carotenoid-9',10'-cleaving dioxygenase
EC 1.13.11.72 2-hydroxyethylphosphonate dioxygenase
EC 1.13.11.73 methylphosphonate synthase
EC 1.13.11.74 2-aminophenol 1,6-dioxygenase
EC 1.13.11.75 all-trans-8'-apo-β-carotenal 15,15'-oxygenase
EC 1.13.11.76 2-amino-5-chlorophenol 1,6-dioxygenase
EC 1.13.11.77 oleate 10S-lipoxygenase
EC 1.13.11.78 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming)
EC 1.13.11.79 5,6-dimethylbenzimidazole synthase
EC 1.13.11.80 (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
EC 1.13.11.81 7,8-dihydroneopterin oxygenase
EC 1.13.11.82 8'-apo-carotenoid 13,14-cleaving dioxygenase


EC 1.13.11.1

Accepted name: catechol 1,2-dioxygenase

Reaction: catechol + O2 = cis,cis-muconate

For diagram click here.

Other name(s): catechol-oxygen 1,2-oxidoreductase; 1,2-pyrocatechase; catechase; catechol 1,2-oxygenase; catechol dioxygenase; pyrocatechase; pyrocatechol 1,2-dioxygenase; CD I; CD II

Systematic name: catechol:oxygen 1,2-oxidoreductase

Comments: Requires Fe3+. Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9027-16-1

References:

1. Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.

2. Hayaishi, O., Katagiri, M. and Rothberg, S. Studies on oxygenases: pyrocatechase. J. Biol. Chem. 229 (1957) 905-920.

3. Sistrom, W.R. and Stanier, R.Y. The mechanism of formation of β-ketoadipic acid by bacteria. J. Biol. Chem. 210 (1954) 821-836.

4. Zeyer, J., Kocher, H.P. and Timmis, N.Influence of para-substituents on the oxidative metabolism of o-nitrophenols by Pseudomonas putida B2. Appl. Environ. Microbiol. 52 (1986) 334-339. [PMID: 3752997]

[EC 1.13.11.1 created 1961 as EC 1.99.2.2, transferred 1965 to EC 1.13.1.1, transferred 1972 to EC 1.13.11.1]

EC 1.13.11.2

Accepted name: catechol 2,3-dioxygenase

misc/catechol Reaction: catechol + O2 = 2-hydroxymuconate-6-semialdehyde

For diagram of reaction click here.

Glossary: 2-hydroxymuconate-6-semialdehyde = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate

Other name(s): 2,3-pyrocatechase; catechol 2,3-oxygenase; catechol oxygenase; metapyrocatechase; pyrocatechol 2,3-dioxygenase; xylE (gene name)

Systematic name: catechol:oxygen 2,3-oxidoreductase (decyclizing)

Comments: Requires FeII. The enzyme initiates the meta-cleavage pathway of catechol degradation.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9029-46-3

References:

1. Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 353-371.

2. Kojima, Y., Itada, N. and Hayaishi, O. Metapyrocatechase: a new catechol-cleaving enzyme. J. Biol. Chem. 236 (1961) 2223-2228. [PMID: 13757654]

3. Nozaki, M., Kagamiyama, H. and Hayaishi, O. Metapyrocatechase. I. Purification, crystallization and some properties. Biochem. Z. 338 (1963) 582-590. [PMID: 14087325]

4. Nakai, C., Hori, K., Kagamiyama, H., Nakazawa, T. and Nozaki, M. Purification, subunit structure, and partial amino acid sequence of metapyrocatechase. J. Biol. Chem. 258 (1983) 2916-2922. [PMID: 6826545]

5. Junker, F., Field, J.A., Bangerter, F., Ramsteiner, K., Kohler, H.-P., Joannou, C.L., Mason, J.R., Leisinger, T. and Cook, A.M. Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid. Biochem. J. 300 (1994) 429-436. [PMID: 8002948]

6. Junker, F., Leisinger, T. and Cook, A.M. 3-Sulphocatechol 2,3-dioxygenase and other dioxygenases (EC 1.13.11.2 and EC 1.14.12.-) in the degradative pathways of 2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic acids in Alcaligenes sp. strain O-1. Microbiology 140 (1994) 1713-1722. [PMID: 8075807]

[EC 1.13.11.2 created 1965 as EC 1.13.1.2, transferred 1972 to EC 1.13.11.2, modified 1999, modified 2013]

EC 1.13.11.3

Accepted name: protocatechuate 3,4-dioxygenase

Reaction: 3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate

For diagram click here.

Glossary: 3,4-dihydroxybenzoate = protocatechuate

Other name(s): protocatechuate oxygenase; protocatechuic acid oxidase; protocatechuic 3,4-dioxygenase; protocatechuic 3,4-oxygenase

Systematic name: protocatechuate:oxygen 3,4-oxidoreductase (decyclizing)

Comments: Requires Fe3+. The enzyme, which participates in the degradation of aromatic compounds, catalyses the intradiol addition of both oxygen atoms from molecular oxygen, resulting in ortho-cleavage of the aromatic ring. The type of cleavage leads to mineralization via the intermediate 3-oxoadipate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9029-47-4

References:

1. Fujisawa, H. and Hayaishi, O. Protocatechuate 3,4-dioxygenase. I. Crystallization and characterization. J. Biol. Chem. 243 (1968) 2673-2681. [PMID: 4967959]

2. Gross, S.R., Gafford, R.D. and Tatum, E.L. The metabolism of protocatechuic acid by Neurospora.J. Biol. Chem. 219 (1956) 781-796.

3. Stanier, R.Y. and Ingraham, J.L. Protocatechuic acid oxidase. J. Biol. Chem. 210 (1954) 799-820.

[EC 1.13.11.3 created 1961 as EC 1.99.2.3, transferred 1965 to EC 1.13.1.3, transferred 1972 to EC 1.13.11.3]

EC 1.13.11.4

Accepted name: gentisate 1,2-dioxygenase

Reaction: 2,5-dihydroxybenzoate + O2 = maleylpyruvate

Other name(s): gentisate oxygenase; 2,5-dihydroxybenzoate dioxygenase; gentisate dioxygenase; gentisic acid oxidase

Systematic name: gentisate:oxygen 1,2-oxidoreductase (decyclizing)

Comments: Requires Fe2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-48-5

References:

1. Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.

2. Sugiyama, S., Yano, K., Komagata, K. and Arima, K. Metabolites of aromatic compounds by microbes. Part VII. Gentisic acid oxidase. Bull. Agric. Chem. Soc. Jpn 24 (1960) 243-248.

3. Sugiyama, S., Yano, K. and Arima, K. Metabolites of aromatic compounds by microbes. Part VII. Further studies of gentisic acid oxidase. Bull. Agric. Chem. Soc. Jpn 24 (1960) 249-254.

[EC 1.13.11.4 created 1961 as EC 1.99.2.4, transferred 1965 to EC 1.13.1.4, transferred 1972 to EC 1.13.11.4]

EC 1.13.11.5

Accepted name: homogentisate 1,2-dioxygenase

Reaction: homogentisate + O2 = 4-maleylacetoacetate

Other name(s): homogentisicase; homogentisate oxygenase; homogentisate dioxygenase; homogentisate oxidase; homogentisic acid oxidase; homogentisic acid oxygenase; homogentisic oxygenase

Systematic name: homogentisate:oxygen 1,2-oxidoreductase (decyclizing)

Comments: Requires Fe2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9029-49-6

References:

1. Adachi, K., Iwayama, Y., Tanioka, H. and Takeda, Y. Purification and properties of homogentisate oxygenase from Pseudomonas fluorescens. Biochim. Biophys. Acta 118 (1966) 88-97. [PMID: 5954067]

2. Crandall, D.I. and Halikis, D.N. Homogentisic acid oxidase. I. Distribution in animal tissues and relation to tyrosine metabolism in rat kidney. J. Biol. Chem. 208 (1954) 629-638.

3. Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.

4. Kita, H., Kamimoto, M., Senoh, S., Adachi, T. and Takeda, Y. Cystallization and some properties of 3,4-dihydroxyphenylacetate-2,3-oxygenase. Biochem. Biophys. Res. Commun. 18 (1965) 66-70.

5. Knox, W.E. and Edwards, S.W. Homogentisate oxidase of liver. J. Biol. Chem. 216 (1955) 479-487.

6. Ravdin, R.G. and Crandall, D.I. The enzymatic conversion of homogentisic acid to 4-fumarylacetoacetic acid. J. Biol. Chem. 189 (1951) 137-149.

[EC 1.13.11.5 created 1961 as EC 1.99.2.5, transferred 1965 to EC 1.13.1.5, transferred 1972 to EC 1.13.11.5]

EC 1.13.11.6

Accepted name: 3-hydroxyanthranilate 3,4-dioxygenase

Reaction: 3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

For diagram of reaction click here.

Other name(s): 3-hydroxyanthranilate oxygenase; 3-hydroxyanthranilic acid oxygenase; 3-hydroxyanthranilic oxygenase; 3-hydroxyanthranilic acid oxidase; 3HAO

Systematic name: 3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing)

Comments: Requires Fe2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9029-50-9

References:

1. Decker, R.H., Kang, H.H., Leach, F.R. and Henderson, L.M. Purification and properties of 3-hydroxyanthranilic acid oxidase. J. Biol. Chem. 236 (1961) 3076-3082.

2. Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.

[EC 1.13.11.6 created 1965 as EC 1.13.1.6, transferred 1972 to EC 1.13.11.6]

[EC 1.13.11.7 Deleted entry: 3,4-dihydroxyphenylacetate 3,4-dioxygenase (EC 1.13.11.7 created 1965 as EC 1.13.1.7, transferred 1972 to EC 1.13.11.7, deleted 1980)]

EC 1.13.11.8

Accepted name: protocatechuate 4,5-dioxygenase

Reaction: protocatechuate + O2 = 4-carboxy-2-hydroxymuconate semialdehyde; protocatechuate:oxygen 4,5-oxidoreductase (decyclizing)

For diagram of reaction click here

Other name(s): protocatechuate 4,5-oxygenase; protocatechuic 4,5-dioxygenase; protocatechuic 4,5-oxygenase

Systematic name: protocatechuate:oxygen 4,5-oxidoreductase (ring-opening)

Comments: Requires Fe2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9029-56-5

References:

1. Trippett, S., Dagley, S. and Stopher, D.A. The bacterial oxidation of nicotinic acid Biochem. J. 76 (1960) 9P.

[EC 1.13.11.8 created 1965 as EC 1.13.1.8, transferred 1972 to EC 1.13.11.8]

EC 1.13.11.9

Accepted name: 2,5-dihydroxypyridine 5,6-dioxygenase

Reaction: 2,5-dihydroxypyridine + O2 = N-formylmaleamic acid

Other name(s): 2,5-dihydroxypyridine oxygenase; pyridine-2,5-diol dioxygenase; NicX

Systematic name: 2,5-dihydroxypyridine:oxygen 5,6-oxidoreductase

Comments: Requires Fe2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 9029-57-6

References:

1. Behrman, E.J. and Stanier, R.Y. The bacterial oxidation of nicotinic acid. J. Biol. Chem. 228 (1957) 923-945. [PMID: 13475371]

2. Gauthier, J.J. and Rittenberg, S.C. The metabolism of nicotinic acid. I. Purification and properties of 2,5-dihydroxypyridine oxygenase from Pseudomonas putida N-9. J. Biol. Chem. 246 (1971) 3737-3742. [PMID: 5578917]

3. Gauthier, J.J. and Rittenberg, S.C. The metabolism of nicotinic acid. II. 2,5-Dihydroxypyridine oxidation, product formation, and oxygen 18 incorporation. J. Biol. Chem. 246 (1971) 3743-3748. [PMID: 5578918]

4. Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440. Proc. Natl. Acad. Sci. USA 105 (2008) 11329-11334. [PMID: 18678916]

[EC 1.13.11.9 created 1965 as EC 1.13.1.9, transferred 1972 to EC 1.13.11.9, modified 2010]

EC 1.13.11.10

Accepted name: 7,8-dihydroxykynurenate 8,8a-dioxygenase

Reaction: 7,8-dihydroxykynurenate + O2 = 5-(3-carboxy-3-oxopropenyl)-4,6-dihydroxypyridine-2-carboxylate

Other name(s): 7,8-dihydroxykynurenate oxygenase; 7,8-dihydroxykynurenate 8,8α-dioxygenase; 7,8-dihydroxykynurenate:oxygen 8,8a-oxidoreductase (decyclizing)

Systematic name: 7,8-dihydroxykynurenate:oxygen 8,8a-oxidoreductase (ring-opening)

Comments: Requires Fe2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-58-7

References:

1. Kuno, S., Tashiro, M., Taniuchi, H., Horibata, K., Hayaishi, O., Seno, S., Tokuyama, T. and Sakan, T. Enzymatic degradation of kynurenic acid. Fed. Proc. 20 (1961) 3.

[EC 1.13.11.10 created 1965 as EC 1.13.1.10, transferred 1972 to EC 1.13.11.10]

EC 1.13.11.11

Accepted name: tryptophan 2,3-dioxygenase

Reaction: L-tryptophan + O2 = N-formyl-L-kynurenine

For diagram, click here

Other name(s): tryptophan pyrrolase (ambiguous); tryptophanase; tryptophan oxygenase; tryptamine 2,3-dioxygenase; tryptophan peroxidase; indoleamine 2,3-dioxygenase (ambiguous); indolamine 2,3-dioxygenase (ambiguous); L-tryptophan pyrrolase; TDO; L-tryptophan 2,3-dioxygenase; L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)

Systematic name: L-tryptophan:oxygen 2,3-oxidoreductase (ring-opening)

Comments: A protohemoprotein. In mammals, the enzyme appears to be located only in the liver. This enzyme, together with EC 1.13.11.52, indoleamine 2,3-dioxygenase, catalyses the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism [5]. The enzyme is specific for tryptophan as substrate, but is far more active with L-tryptophan than with D-tryptophan [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9014-51-1

References:

1. Uchida, K., Shimizu, T., Makino, R., Sakaguchi, K., Iizuka, T., Ishimura, Y., Nozawa, T. and Hatano, M. Magnetic and natural circular dichroism of L-tryptophan 2,3-dioxygenases and indoleamine 2,3-dioxygenase. I. Spectra of ferric and ferrous high spin forms. J. Biol. Chem. 258 (1983) 2519-2525. [PMID: 6600455]

2. Ren, S., Liu, H., Licad, E. and Correia, M.A. Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme. Arch. Biochem. Biophys. 333 (1996) 96-102. [PMID: 8806758]

3. Leeds, J.M., Brown, P.J., McGeehan, G.M., Brown, F.K. and Wiseman, J.S. Isotope effects and alternative substrate reactivities for tryptophan 2,3-dioxygenase. J. Biol. Chem. 268 (1993) 17781-17786. [PMID: 8349662]

4. Dang, Y., Dale, W.E. and Brown, O.R. Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway. Free Radic. Biol. Med. 28 (2000) 615-624. [PMID: 10719243]

5. Littlejohn, T.K., Takikawa, O., Truscott, R.J. and Walker, M.J. Asp274 and His346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase. J. Biol. Chem. 278 (2003) 29525-29531. [PMID: 12766158]

[EC 1.13.11.11 created 1961 as EC 1.11.1.4, deleted 1964, reinstated 1965 as EC 1.13.1.12, transferred 1972 to EC 1.13.11.11, modified 1989, modified 2006]

EC 1.13.11.12

Accepted name: linoleate 13S-lipoxygenase

Reaction: (1) linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
(2) α-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate

Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate
α-linolenate = (9Z,12Z,15Z)-octadeca-9,12,15-trienoate

Other name(s): 13-lipoxidase; carotene oxidase; 13-lipoperoxidase; fat oxidase; 13-lipoxydase; lionoleate:O2 13-oxidoreductase

Systematic name: linoleate:oxygen 13-oxidoreductase

Comments: Contains nonheme iron. A common plant lipoxygenase that oxidizes linoleate and α-linolenate, the two most common polyunsaturated fatty acids in plants, by inserting molecular oxygen at the C-13 position with (S)-configuration. This enzyme produces precursors for several important compounds, including the plant hormone jasmonic acid. EC 1.13.11.58, linoleate 9S-lipoxygenase, catalyses a similar reaction at the second available position of these fatty acids.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-60-1

References:

1. Christopher, J., Pistorius, E. and Axelrod, B. Isolation of an enzyme of soybean lipoxidase. Biochim. Biophys. Acta 198 (1970) 12-19. [PMID: 5461103]

2. Theorell, H., Holman, R.T. and Åkesson, Å. Crystalline lipoxidase. Acta Chem. Scand. 1 (1947) 571-576. [PMID: 18907700]

3. Zimmerman, D.C. Specificity of flaxseed lipoxidase. Lipids 5 (1970) 392-397. [PMID: 5447012]

4. Royo, J., Vancanneyt, G., Perez, A.G., Sanz, C., Stormann, K., Rosahl, S. and Sanchez-Serrano, J.J. Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns. J. Biol. Chem. 271 (1996) 21012-21019. [PMID: 8702864]

5. Bachmann, A., Hause, B., Maucher, H., Garbe, E., Voros, K., Weichert, H., Wasternack, C. and Feussner, I. Jasmonate-induced lipid peroxidation in barley leaves initiated by distinct 13-LOX forms of chloroplasts. Biol. Chem. 383 (2002) 1645-1657. [PMID: 12452441]

[EC 1.13.11.12 created 1961 as EC 1.99.2.1, transferred 1965 to EC 1.13.1.13, transferred 1972 to EC 1.13.11.12, modified 2011, modified 2012]

[EC 1.13.11.13 Deleted entry: ascorbate 2,3-dioxygenase. The activity is the sum of several enzymatic and spontaneous reactions (EC 1.13.11.13 created 1972, deleted 2012)]

EC 1.13.11.14

Accepted name: 2,3-dihydroxybenzoate 3,4-dioxygenase

Reaction: 2,3-dihydroxybenzoate + O2 = 3-carboxy-2-hydroxymuconate semialdehyde

Other name(s): o-pyrocatechuate oxygenase; 2,3-dihydroxybenzoate 1,2-dioxygenase; 2,3-dihydroxybenzoic oxygenase; 2,3-dihydroxybenzoate oxygenase; 2,3-dihydroxybenzoate:oxygen 3,4-oxidoreductase (decyclizing)

Systematic name: 2,3-dihydroxybenzoate:oxygen 3,4-oxidoreductase (ring-opening)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9032-31-9

References:

1. Ribbons, D.W. Bacterial oxidation of 2,3-dihydroxybenzoic acid - a new oxygenase. Biochem. J. 99 (1966) 30P-31P.

[EC 1.13.11.14 created 1972, modified 1976]

EC 1.13.11.15

Accepted name: 3,4-dihydroxyphenylacetate 2,3-dioxygenase

Reaction: 3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde

Other name(s): 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase; HPC dioxygenase; homoprotocatechuate 2,3-dioxygenase;3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (decyclizing)

Systematic name: 3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (ring-opening)

Comments: An iron protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 37256-56-7

References:

1. Adachi, K., Takeda, Y., Senoh, S. and Kita, H. Metabolism of p-hydroxyphenylacetic acid in Pseudomonas ovalis. Biochim. Biophys. Acta 93 (1964) 483-493.

2. Barbour, M.G. and Bayly, R.C. Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida. J. Bacteriol. 147 (1981) 844-850. [PMID: 5891457]

3. Krishnan Kutty, R., Devi, N.A., Veeraswamy, M., Ramesh, S. and Subba Rao, P.V. Degradation of (+/-)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde. Biochem. J. 167 (1977) 163-170. [PMID: 588248]

[EC 1.13.11.15 created 1972]

EC 1.13.11.16

Accepted name: 3-carboxyethylcatechol 2,3-dioxygenase

Reaction: (1) 3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
(2) (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate

For diagram of reaction click here or click here.

Glossary: (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate = trans-2,3-dihydroxycinnamate

Other name(s): 2,3-dihydroxy-β-phenylpropionic dioxygenase; 2,3-dihydroxy-β-phenylpropionate oxygenase; 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase; 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase (decyclizing)

Systematic name: 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase (ring-opening)

Comments: An iron protein. This enzyme catalyses a step in the pathway of phenylpropanoid compounds degradation.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 105503-63-7

References:

1. Dagley, S., Chapman, P.J. and Gibson, D.T. The metabolism of β-phenylpropionic acid by an Achromobacter. Biochem. J. 97 (1965) 643-650. [PMID: 5881653]

2. Lam, W. W. Y and Bugg, T. D. H. Chemistry of extradiol aromatic ring cleavage: isolation of a stable dienol ring fission intermediate and stereochemistry of its enzymatic hydrolytic clevage. J. Chem. Soc., Chem. Commun. 10 (1994) 1163-1164.

3. Díaz, E., Ferrández, A. and García, J.L. Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12. J. Bacteriol. 180 (1998) 2915-2923. [PMID: 9603882]

[EC 1.13.11.16 created 1972, modified 2011, modified 2012]

EC 1.13.11.17

Accepted name: indole 2,3-dioxygenase

Reaction: indole + O2 = 2-formylaminobenzaldehyde

Other name(s): indole oxidase; indoleamine 2,3-dioxygenase (ambiguous); indole:O2 oxidoreductase ; indole-oxygen 2,3-oxidoreductase (decyclizing); IDO (ambiguous); indole:oxygen 2,3-oxidoreductase (decyclizing)

Systematic name: indole:oxygen 2,3-oxidoreductase (ring-opening)

Comments: Enzymes from the plants Tecoma stans, Jasminum grandiflorum and Zea mays are flavoproteins containing copper. They are part of enzyme systems that form either anthranil (2,1-benzoisoxazole) (Tecoma stans), anthranilate (Jasminum grandiflorum) or both (Zea mays) as the final product. A second enzyme from Tecoma stans is not a flavoprotein, does not require copper, and is part of a system that forms anthranilate as the final product.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-57-8

References:

1. Divakar, N.G., Subramanian, V., Sugumaran, M. and Vaidyanathan, C.S. Indole oxygenase from the leaves of Jasminum grandiflorum. Plant Sci. Lett. 15 (1979) 177-181.

2. Chauhan, Y.S., Rathore, V.S., Garg, G.K. and Bhargava, A. Detection of an indole oxidizing system in maize leaves. Biochem. Biophys. Res. Commun. 83 (1978) 1237-1245. [PMID: 697856]

3. Nair, P.M. and Vaidyanathan, C.S. An indole oxidase isolated from the leaves of Tecoma stans. Biochim. Biophys. Acta 81 (1964) 496-506.

4. Kunapuli, S.P. and Vaidyanathan, C.S. Purification and characterization of a new indole oxygenase from the leaves of Tecoma stans L. Plant Physiol. 71 (1983) 19-23. [PMID: 16662784]

[EC 1.13.11.17 created 1972, modified 1986]

EC 1.13.11.18

Accepted name: persulfide dioxygenase

Reaction: S-sulfanylglutathione + O2 + H2O = glutathione + sulfite + 2 H+ (overall reaction)
(1a) S-sulfanylglutathione + O2 = S-sulfinatoglutathione + H+
(1b) S-sulfinatoglutathione + H2O = glutathione + sulfite + H+ (spontaneous)

Other name(s): sulfur oxygenase (incorrect); sulfur:oxygen oxidoreductase (incorrect); sulfur dioxygenase (incorrect)

Systematic name: S-sulfanylglutathione:oxygen oxidoreductase

Comments: An iron protein. Perthiols, formed spontaneously by interactions between thiols and elemental sulfur or sulfide, are the only acceptable substrate to the enzyme. The sulfite that is formed by the enzyme can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically [2].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-58-9

References:

1. Suzuki, I. and Silver, M. The initial product and properties of the sulfur-oxidizing enzyme of thiobacilli. Biochim. Biophys. Acta 122 (1966) 22-33. [PMID: 5968172]

2. Rohwerder, T. and Sand, W. The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp. Microbiology 149 (2003) 1699-1710. [PMID: 12855721]

3. Liu, H., Xin, Y. and Xun, L. Distribution, diversity, and activities of sulfur dioxygenases in heterotrophic bacteria. Appl. Environ. Microbiol. 80 (2014) 1799-1806. [PMID: 24389926]

4. Holdorf, M.M., Owen, H.A., Lieber, S.R., Yuan, L., Adams, N., Dabney-Smith, C. and Makaroff, C.A. Arabidopsis ETHE1 encodes a sulfur dioxygenase that is essential for embryo and endosperm development. Plant Physiol. 160 (2012) 226-236. [PMID: 22786886]

5. Pettinati, I., Brem, J., McDonough, M.A. and Schofield, C.J. Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy. Hum. Mol. Genet. 24 (2015) 2458-2469. [PMID: 25596185]

[EC 1.13.11.18 created 1972, modified 2015]

EC 1.13.11.19

Accepted name: cysteamine dioxygenase

Reaction: 2-aminoethanethiol + O2 = hypotaurine

For diagram, click here

Other name(s): persulfurase; cysteamine oxygenase; cysteamine:oxygen oxidoreductase

Systematic name: 2-aminoethanethiol:oxygen oxidoreductase

Comments: A non-heme iron protein that is involved in the biosynthesis of taurine. Requires catalytic amounts of a cofactor-like compound, such as sulfur, sufide, selenium or methylene blue for maximal activity. 3-Aminopropanethiol (homocysteamine) and 2-mercaptoethanol can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates [1,3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9033-41-4

References:

1. Cavallini, D., de Marco, C., Scandurra, R., Duprè, S. and Graziani, M.T. The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme. J. Biol. Chem. 241 (1966) 3189-3196. [PMID: 5912113]

2. Wood, J.L. and Cavallini, D. Enzymic oxidation of cysteamine to hypotaurine in the absence of a cofactor. Arch. Biochem. Biophys. 119 (1967) 368-372. [PMID: 6052430]

3. Cavallini, D., Federici, G., Ricci, G., Duprè, S. and Antonucci, A. The specificity of cysteamine oxygenase. FEBS Lett. 56 (1975) 348-351. [PMID: 1157952]

4. Richerson, R.B. and Ziegler, D.M. Cysteamine dioxygenase. Methods Enzymol. 143 (1987) 410-415. [PMID: 3657558]

[EC 1.13.11.19 created 1972, modified 2006]

EC 1.13.11.20

Accepted name: cysteine dioxygenase

Reaction: L-cysteine + O2 = 3-sulfinoalanine

For diagram click here.

Other name(s): cysteine oxidase

Systematic name: L-cysteine:oxygen oxidoreductase

Comments: Requires Fe2+ and NAD(P)H.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37256-59-0

References:

1. Lombardini, J.B., Singer, T.P. and Boyer, P.D. Cystein oxygenase. II. Studies on the mechanism of the reaction with 18oxygen. J. Biol. Chem. 244 (1969) 1172-1175. [PMID: 5767301]

[EC 1.13.11.20 created 1972, modified 1976]

[EC 1.13.11.21 Transferred entry: now EC 1.14.99.36, β-carotene 15,15'-monooxygenase (EC 1.13.11.21 created 1972, deleted 2001)]

EC 1.13.11.22

Accepted name: caffeate 3,4-dioxygenase

Reaction: 3,4-dihydroxy-trans-cinnamate + O2 = 3-(2-carboxyethenyl)-cis,cis-muconate; 3,4-dihydroxy-trans-cinnamate:oxygen 3,4-oxidoreductase (decyclizing)

Systematic name: 3,4-dihydroxy-trans-cinnamate:oxygen 3,4-oxidoreductase (ring-opening)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-61-4

References:

1. Seidman, M.M., Toms, A. and Wood, J.M. Influence of side-chain substituents on the position of cleavage of the benzene ring by Pseudomonas fluorescens. J. Bacteriol. 97 (1969) 1192-1197. [PMID: 5776526]

[EC 1.13.11.22 created 1972]

EC 1.13.11.23

Accepted name: 2,3-dihydroxyindole 2,3-dioxygenase

Reaction: 2,3-dihydroxyindole + O2 = anthranilate + CO2

Other name(s): 2,3-dihydroxyindole:oxygen 2,3-oxidoreductase (decyclizing)

Systematic name: 2,3-dihydroxyindole:oxygen 2,3-oxidoreductase (ring-opening)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-62-5

References:

1. Fujioka, M. and Wada, H. The bacterial oxidation of indole. Biochim. Biophys. Acta 158 (1968) 70-78. [PMID: 5652436]

[EC 1.13.11.23 created 1972]

EC 1.13.11.24

Accepted name: quercetin 2,3-dioxygenase

Reaction: quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+

For diagram of reaction click here

Other name(s): quercetinase; flavonol 2,4-oxygenase; quercetin:oxygen 2,3-oxidoreductase (decyclizing)

Systematic name: quercetin:oxygen 2,3-oxidoreductase (ring-opening)

Comments: The enzyme from Aspergillus sp. is a copper protein whereas that from Bacillus subtilis contains iron. Quercetin is a flavonol (5,7,3',4'-tetrahydroxyflavonol).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9075-67-6

References:

1. Oka, T. and Simpson, F.J. Quercetinase, a dioxygenase containing copper. Biochem. Biophys. Res. Commun. 43 (1971) 1-5. [PMID: 5579942]

2. Steiner, R.A., Kalk, K.H. and Dijkstra, B.W. Anaerobic enzyme·substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. Proc. Natl. Acad. Sci. USA 99 (2002) 16625-16630. [PMID: 12486225]

3. Bowater, L., Fairhurst, S.A., Just, V.J., and Bornemann, S. Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase. FEBS Lett. 557 (2004) 45-48. [PMID: 14741339]

[EC 1.13.11.24 created 1972]

EC 1.13.11.25

Accepted name: 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase

Reaction: 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + O2 = 3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate

Other name(s): steroid 4,5-dioxygenase; 3-alkylcatechol 2,3-dioxygenase; 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione:oxygen 4,5-oxidoreductase (decyclizing)

Systematic name: 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione:oxygen 4,5-oxidoreductase (ring-opening)

Comments: Requires Fe2+. Also acts on 3-isopropylcatechol and 3-tert-butyl-5-methylcatechol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37256-63-6

References:

1. Gibson, D.T., Wang, K.C., Sih, C.J. and Whitlock, J.H. Mechanisms of steroid oxidation by microorganisms. IX. On the mechanism of ring A cleavage in the degradation of 9,10-seco steroids by microorganisms. J. Biol. Chem. 241 (1966) 551-559. [PMID: 5908121]

[EC 1.13.11.25 created 1972]

EC 1.13.11.26

Accepted name: peptide-tryptophan 2,3-dioxygenase

Reaction: [protein]-L-tryptophan + O2 = [protein]-N-formyl-L-kynurenine

Glossary: N-formyl-L-kynurenine = (2S)-2-amino-4-[2-(formamido)phenyl]-4-oxobutanoic acid

Other name(s): pyrrolooxygenase; peptidyltryptophan 2,3-dioxygenase; tryptophan pyrrolooxygenase; [protein]-L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)

Systematic name: [protein]-L-tryptophan:oxygen 2,3-oxidoreductase (ring-opening)

Comments: Also acts on tryptophan.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-64-7

References:

1. Frydman, R.B., Tomaro, M.L. and Frydman, B. Pyrrolooxygenase: its action on tryptophan-containing enzymes and peptides. Biochim. Biophys. Acta 284 (1972) 80-89. [PMID: 4403729]

2. Camoretti-Mercado, B. and Frydman, R.B. Separation of tryptophan pyrrolooxygenase into three molecular forms. A study of their substrate specificities using tryptophyl-containing peptides and proteins. Eur. J. Biochem. 156 (1986) 317-325. [PMID: 3699018]

[EC 1.13.11.26 created 1972, modified 2011]

EC 1.13.11.27

Accepted name: 4-hydroxyphenylpyruvate dioxygenase

Reaction: 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2

For diagram of reaction click here.

Other name(s): p-hydroxyphenylpyruvic hydroxylase; p-hydroxyphenylpyruvate hydroxylase; p-hydroxyphenylpyruvate oxidase; p-hydroxyphenylpyruvic oxidase; p-hydroxyphenylpyruvate dioxygenase; p-hydroxyphenylpyruvic acid hydroxylase; 4-hydroxyphenylpyruvic acid dioxygenase

Systematic name: 4-hydroxyphenylpyruvate:oxygen oxidoreductase (hydroxylating, decarboxylating)

Comments: The Pseudomonas enzyme contains one Fe3+ per mole of enzyme; the enzymes from other sources may contain essential iron or copper. Formerly EC 1.14.2.2 and EC 1.99.1.14.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9029-72-5

References:

1. Lindstedt, S. and Rundgren, M. Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874. J. Biol. Chem. 257 (1982) 11922-11931. [PMID: 7118918]

2. Roche, P.A., Moorehead, T.J. and Hamilton, G.A. Purification and properties of hog liver 4-hydroxyphenylpyruvate dioxygenase. Arch. Biochem. Biophys. 216 (1982) 62-73. [PMID: 7103516]

[EC 1.13.11.27 created 1961 as EC 1.99.1.14, transferred 1965 to EC 1.14.2.2, transferred 1972 to EC 1.13.11.27]

EC 1.13.11.28

Accepted name: 2,3-dihydroxybenzoate 2,3-dioxygenase

Reaction: 2,3-dihydroxybenzoate + O2 = 2-carboxy-cis,cis-muconate

Other name(s): 2,3-dihydroxybenzoate 2,3-oxygenase; 2,3-dihydroxybenzoate:oxygen 2,3-oxidoreductase (decyclizing)

Systematic name: 2,3-dihydroxybenzoate:oxygen 2,3-oxidoreductase (ring-opening)

Comments: Also acts, more slowly, with 2,3-dihydroxy-4-methylbenzoate and 2,3-dihydroxy-4-isopropylbenzoate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 56802-97-2

References:

1. La Du, B.N. and Zannoni, V.G. The tyrosine oxidation system of liver. III. Further studies on the oxidation of p-hydroxyphenylpyruvic acid. J. Biol. Chem. 219 (1956) 273-281.

2. Sharma, H.K. and Vaidyanathan, C.S. A new mode of ring cleavage of 2,3-dihydroxybenzoic acid in Tecoma stans (L.). Partial purification and properties of 2,3-dihydroxybenzoate 2,3-oxygenase. Eur. J. Biochem. 56 (1975) 163-171. [PMID: 1175620]

[EC 1.13.11.28 created 1978]

EC 1.13.11.29

Accepted name: stizolobate synthase

Reaction: L-dopa + O2 = 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde

Systematic name: 3,4-dihydroxy-L-phenylalanine:oxygen 4,5-oxidoreductase (recyclizing)

Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine

Comments: The intermediate product undergoes ring closure and oxidation, with NAD(P)+ as acceptor, to stizolobic acid. The enzyme requires Zn2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 65979-39-7

References:

1. Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. An enzyme system(s) catalyzing the conversion of dihydroxyphenylalanine into stizolobinic acid and stizolobic acid from etiolated seedlings of Stizolobium hassjoo. Eur. J. Biochem. 68 (1976) 237-243. [PMID: 9285]

2. Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. Eur. J. Biochem. 82 (1978) 385-392. [PMID: 624278]

[EC 1.13.11.29 created 1978]

EC 1.13.11.30

Accepted name: stizolobinate synthase

Reaction: L-dopa + O2 = 5-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde

Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine

Systematic name: 3,4-dihydroxy-L-phenylalanine:oxygen 2,3-oxidoreductase (recyclizing)

Comments: The intermediate product undergoes ring closure and oxidation, with NAD(P)+ as acceptor, to stizolobinic acid. The enzyme requires Zn2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 65979-38-6

References:

1. Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. An enzyme system(s) catalyzing the conversion of dihydroxyphenylalanine into stizolobinic acid and stizolobic acid from etiolated seedlings of Stizolobium hassjoo. Eur. J. Biochem. 68 (1976) 237-243. [PMID: 9285]

2. Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. Eur. J. Biochem. 82 (1978) 385-392. [PMID: 624278]

[EC 1.13.11.30 created 1978]

EC 1.13.11.31

Accepted name: arachidonate 12-lipoxygenase

Reaction: arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate

Other name(s): δ12-lipoxygenase; 12-lipoxygenase; 12δ-lipoxygenase; C-12 lipoxygenase; 12S-lipoxygenase; leukotriene A4 synthase; LTA4 synthase

Systematic name: arachidonate:oxygen 12-oxidoreductase

Comments: The product is rapidly reduced to the corresponding 12S-hydroxy compound.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 82391-43-3

References:

1. Hamberg, M. and Samuelsson, B. Prostaglandin endoperoxides. Novel transformations of arachidonic acid in human platelets. Proc. Natl. Acad. Sci. USA 71 (1974) 3400-3404. [PMID: 4215079]

2. Nugteren, D.H. Arachidonate lipoxygenase in blood platelets. Biochim. Biophys. Acta 380 (1975) 299-307. [PMID: 804329]

3. Wallach, D.P. and Brown, V.R. A novel preparation of human platelet lipoxygenase. Characteristics and inhibition by a variety of phenyl hydrazones and comparisons with other lipoxygenases. Biochim. Biophys. Acta 663 (1981) 361-372. [PMID: 6783111]

[EC 1.13.11.31 created 1983]

[EC 1.13.11.32 Transferred entry: 2-nitropropane dioxygenase. Now EC 1.13.12.16, nitronate monooxygenase. (EC 1.13.11.32 created 1984, modified 2006, deleted 2009)]

EC 1.13.11.33

Accepted name: arachidonate 15-lipoxygenase

Reaction: arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate

Other name(s): 15-lipoxygenase; linoleic acid ω6-lipoxygenase; ω6 lipoxygenase

Systematic name: arachidonate:oxygen 15-oxidoreductase

Comments: The product is rapidly reduced to the corresponding 15S-hydroxy compound.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 82249-77-2

References:

1. Bryant, R.W., Bailey, J.M., Schewqe, T. and Rapoport, S.M. Positional specificity of a reticulocyte lipoxygenase. Conversion of arachidonic acid to 15-S-hydroperoxy-eicosatetraenoic acid. J. Biol. Chem. 257 (1982) 6050-6055. [PMID: 6804460]

2. Narumiya, S. and Salmon, J.A. Arachidonic acid-15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. Methods Enzymol. 86 (1982) 45-48. [PMID: 6813644]

3. Oliw, E.H. and Sprecher, H. Metabolism of polyunsaturated fatty acids by an (n-6)-lipoxygenase associated with human ejaculates. Biochim. Biophys. Acta 1002 (1989) 283-291. [PMID: 2496760]

4. Shibata, D., Steczko, J., Dixon, F.E., Hermodson, M., Yasdanparast, R. and Axelrod, B. Primary structure of soybean lipoxygenase-1. J. Biol. Chem. 262 (1987) 10080-10085. [PMID: 3112136]

[EC 1.13.11.33 created 1984]

EC 1.13.11.34

Accepted name: arachidonate 5-lipoxygenase

Reaction: arachidonate + O2 = (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O (overall reaction)
(1a) arachidonate + O2 = (5S,6E,8Z,11Z,14Z)-5-hydroperoxyicosa-6,8,11,14-tetraenoate
(1b) (5S,6E,8Z,11Z,14Z)-5-hydroperoxyicosa-6,8,11,14-tetraenoate = (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O

For diagram of reaction click here

Glossary: leukotriene A4 = (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate

Other name(s): leukotriene-A4 synthase; δ5-lipoxygenase; 5δ-lipoxygenase; arachidonic 5-lipoxygenase; arachidonic acid 5-lipoxygenase; C-5-lipoxygenase; LTA synthase; leukotriene A4 synthase

Systematic name: arachidonate:oxygen 5-oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 80619-02-9

References:

1. Matsumoto, T., Funk, C.D., Radmark, O., Hoog, J.-O., Jornvall, H. and Samuelsson, B. Molecular cloning and amino acid sequence of human 5-lipoxygenase. Proc. Natl. Acad. Sci. USA 85 (1988) 26-30. [PMID: 2829172]

2. Ohishi, N., Izumi, T., Minami, M., Kitamura, S., Seyama, Y., Ohkawa, S., Terao, S., Yotsumoto, H., Takaku, F. and Shimizu, T. Leukotriene A4 hydrolase in the human lung. Inactivation of the enzyme with leukotriene A4 isomers. J. Biol. Chem. 262 (1987) 10200-10205. [PMID: 3038871]

3. Shimizu, T., Izumi, T., Seyama, Y., Tadokoro, K., Rädmark, O. and Samuelsson, B. Characterization of leukotriene A4 synthase from murine mast cells: evidence for its identity to arachidonate 5-lipoxygenase. Proc. Natl. Acad. Sci. USA 83 (1986) 4175-4179. [PMID: 3012557]

4. Shimizu, T., Rädmark, O. and Samuelssohn, B. Enzyme with dual lipoxygenase activities catalyzes leukotriene A4 synthesis from arachidonic acid. Proc. Natl. Acad. Sci. USA 81 (1984) 689-693. [PMID: 6322165]

[EC 1.13.11.34 created 1984, modified 1990]

EC 1.13.11.35

Accepted name: pyrogallol 1,2-oxygenase

Reaction: 1,2,3-trihydroxybenzene + O2 = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate

Glossary: (2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (2Z,4E)-2-hydroxymuconate
1,2,3-trihydroxybenzene = pyrogallol

Other name(s): pyrogallol 1,2-dioxygenase; 1,2,3-trihydroxybenzene:oxygen 1,2-oxidoreductase (decyclizing)

Systematic name: 1,2,3-trihydroxybenzene:oxygen 1,2-oxidoreductase (ring-opening)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 78310-68-6

References:

1. Groseclose, E.E. and Ribbons, D.W. Metabolism of resorcinylic compounds by bacteria: new pathway for resorcinol catabolism in Azotobacter vinelandii. J. Bacteriol. 146 (1981) 460-466. [PMID: 7217008]

[EC 1.13.11.35 created 1984, modified 2012]

EC 1.13.11.36

Accepted name: chloridazon-catechol dioxygenase

Reaction: 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2 = 5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone

Other name(s): 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone 1,2-oxidoreductase (decyclizing)

Systematic name: 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone 1,2-oxidoreductase (ring-opening)

Comments: An iron protein, requiring additional Fe2+. Not identical with EC 1.13.11.1 (catechol 1,2-dioxygenase), EC 1.13.11.2 (catechol 2,3-dioxygenase) or EC 1.13.11.5 (homogentisate 1,2-dioxygenase). Involved in the breakdown of the herbicide chloridazon.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 82869-32-7

References:

1. Müller, R, Haug, S., Eberspächer, J. and Lingens, F. Catechol-2,3-Dioxygenase aus Pyrazon-abbauenden Bakterien. Hoppe-Seyler's Z. Physiol. Chem. 358 (1977) 797-805. [PMID: 19349]

2. Müller, R., Schmitt, S. and Lingens, F. A novel non-heme iron-containing dioxygenase. Chloridazon-catechol dioxygenase from Phenylobacterium immobilis DSM 1986. Eur. J. Biochem. 125 (1982) 579-584. [PMID: 6811270]

[EC 1.13.11.36 created 1984]

EC 1.13.11.37

Accepted name: hydroxyquinol 1,2-dioxygenase

Reaction: hydroxyquinol + O2 = maleylacetate

For diagram of reaction click here.

Glossary: hydroxyquinol = 1,2,4-trihydroxybenzene
maleylacetate = (2Z)-4-oxohex-2-enedioate
Other name(s): hydroxyquinol dioxygenase; benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (decyclizing)

Systematic name: benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (ring-opening)

Comments: An iron protein. Highly specific; catechol and pyrogallol are acted on at less than 1% of the rate at which hydroxyquinol is oxidized.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 91847-14-2

References:

1. Sze, I.S.-Y. and Dagley, S. Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum. J. Bacteriol. 159 (1984) 353-359. [PMID: 6539772]

2. Ferraroni, M., Seifert, J., Travkin, V.M., Thiel, M., Kaschabek, S., Scozzafava, A., Golovleva, L., Schlomann, M. and Briganti, F. Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation. J. Biol. Chem. 280 (2005) 21144-21154. [PMID: 15772073]

3. Hatta, T., Nakano, O., Imai, N., Takizawa, N. and Kiyohara, H. Cloning and sequence analysis of hydroxyquinol 1,2-dioxygenase gene in 2,4,6-trichlorophenol-degrading Ralstonia pickettii DTP0602 and characterization of its product. J. Biosci. Bioeng. 87 (1999) 267-272. [PMID: 16232466]

[EC 1.13.11.37 created 1989, modified 2013]

EC 1.13.11.38

Accepted name: 1-hydroxy-2-naphthoate 1,2-dioxygenase

Reaction: 1-hydroxy-2-naphthoate + O2 = (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate

For diagram of reaction click here

Other name(s): 1-hydroxy-2-naphthoate dioxygenase; 1-hydroxy-2-naphthoate-degrading enzyme; 1-hydroxy-2-naphthoic acid dioxygenase; 1-hydroxy-2-naphthoate:oxygen 1,2-oxidoreductase (decyclizing)

Systematic name: 1-hydroxy-2-naphthoate:oxygen 1,2-oxidoreductase (ring-opening)

Comments: Requires Fe2+. Involved, with EC 4.1.2.34 4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase, in the metabolism of phenanthrene in bacteria.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 85941-64-6

References:

1. Barnsley, E.A. Phthalate pathway of phenanthrene metabolism: formation of 2'-carboxybenzalpyruvate. J. Bacteriol. 154 (1983) 113-117. [PMID: 6833175]

[EC 1.13.11.38 created 1989]

EC 1.13.11.39

Accepted name: biphenyl-2,3-diol 1,2-dioxygenase

Reaction: biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O

Other name(s): 2,3-dihydroxybiphenyl dioxygenase; biphenyl-2,3-diol dioxygenase; bphC (gene name); biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (decyclizing)

Systematic name: biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (ring-opening)

Comments: Contains Fe2+ or Mn2+ [3]. This enzyme participates in the degradation pathway of biphenyl and PCB (polychlorinated biphenyls), and catalyses the first ring cleavage step by incorporating two atomic oxygens into the catechol ring formed by EC 1.3.1.56, cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase. The enzyme from the bacterium Burkholderia xenovorans LB400 can also process catechol, 3-methylcatechol, and 4-methylcatechol, but less efficiently [1]. The enzyme from the carbazole-degrader Pseudomonas resinovorans strain CA10 also accepts 2'-aminobiphenyl-2,3-diol [5]. The enzyme from the bacterium Ralstonia sp. SBUG 290 can also accept 1,2-dihydroxydibenzofuran and 1,2-dihydroxynaphthalene [4]. The enzyme is strongly inhibited by the substrate [1]. Not identical with EC 1.13.11.2 catechol 2,3-dioxygenase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 103679-58-9

References:

1. Eltis, L.D., Hofmann, B., Hecht, H.J., Lunsdorf, H. and Timmis, K.N. Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase. J. Biol. Chem. 268 (1993) 2727-2732. [PMID: 8428946]

2. Uragami, Y., Senda, T., Sugimoto, K., Sato, N., Nagarajan, V., Masai, E., Fukuda, M. and Mitsu, Y. Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase. J. Inorg. Biochem. 83 (2001) 269-279. [PMID: 11293547]

3. Hatta, T., Mukerjee-Dhar, G., Damborsky, J., Kiyohara, H. and Kimbara, K. Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8. J. Biol. Chem. 278 (2003) 21483-21492. [PMID: 12672826]

4. Wesche, J., Hammer, E., Becher, D., Burchhardt, G. and Schauer, F. The bphC gene-encoded 2,3-dihydroxybiphenyl-1,2-dioxygenase is involved in complete degradation of dibenzofuran by the biphenyl-degrading bacterium Ralstonia sp. SBUG 290. J Appl Microbiol 98 (2005) 635-645. [PMID: 15715866]

5. Iwata, K., Nojiri, H., Shimizu, K., Yoshida, T., Habe, H. and Omori, T. Expression, purification, and characterization of 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase from carbazole-degrader Pseudomonas resinovorans strain CA10. Biosci. Biotechnol. Biochem. 67 (2003) 300-307. [PMID: 12728990]

[EC 1.13.11.39 created 1989, modified 2010]

EC 1.13.11.40

Accepted name: arachidonate 8-lipoxygenase

Reaction: arachidonate + O2 = (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate

Other name(s): 8-lipoxygenase; 8(R)-lipoxygenase

Systematic name: arachidonate:oxygen 8-oxidoreductase

Comments: From the coral Pseudoplexaura porosa.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 100900-72-9

References:

1. Bundy, G.L., Nidy, E.G., Epps, D.E., Mizsak, S.A. and Wnuk, R.J. Discovery of an arachidonic acid C-8 lipoxygenase in the gorgonian coral Pseudoplexaura porosa. J. Biol. Chem. 261 (1986) 747-751. [PMID: 2867091]

[EC 1.13.11.40 created 1989]

EC 1.13.11.41

Accepted name: 2,4'-dihydroxyacetophenone dioxygenase

Reaction: 2,4'-dihydroxyacetophenone + O2 = 4-hydroxybenzoate + formate

Other name(s): (4-hydroxybenzoyl)methanol oxygenase

Systematic name: 2,4'-dihydroxyacetophenone oxidoreductase (C-C-bond-cleaving)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 257617-97-3

References:

1. Hopper, D.J. Oxygenase properties of the (4-hydroxybenzoyl)methanol-cleavage enzyme from an Alcaligenes sp. Biochem. J. 239 (1986) 469-472. [PMID: 3814084]

[EC 1.13.11.41 created 1989]

[EC 1.13.11.42 Deleted entry: indoleamine-pyrrole 2,3-dioxygenase (EC 1.13.11.42 created 1992, deleted 2006)]

EC 1.13.11.43

Accepted name: lignostilbene αβ-dioxygenase

Reaction: 1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O2 = 2 vanillin

Systematic name: 1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene:oxygen oxidoreductase (αβ-bond-cleaving)

Comments: An iron protein. The enzyme catalyses oxidative cleavage of the interphenyl double bond in the synthetic substrate and lignin-derived stilbenes. It is responsible for the degradation of a diarylpropane-type structure in lignin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 124834-28-2

References:

1. Kamoda, S., Habu, N., Samejima, M. and Yoshimoto, T. Purification and some properties of lignostilbene-αβ- dioxygenase responsible for the Cα-Cβ cleavage of a diarylpropane type lignin model-compound from Pseudomonas sp TMY1009. Agric. Biol. Chem. 53 (1989) 2757-2761.

[EC 1.13.11.43 created 1992]

[EC 1.13.11.44 Deleted entry: linoleate diol synthase. Activity is covered by EC 1.13.11.60, linoleate 8R-lipoxygenase and EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase. (EC 1.13.11.44 created 2000, deleted 2011)]

EC 1.13.11.45

Accepted name: linoleate 11-lipoxygenase

Reaction: linoleate + O2 = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate

Glossary:
arachidonate: (all-Z)-icosa-5,8,11,14-tetraenoate
linoleate: (9Z,12Z)-octadeca-9,12-dienoate
α-linolenate: (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
γ-linolenate: (6Z,9Z,12Z)-octadeca-6,9,12-trienoate
oleate: (Z)-octadec-9-enoate

Other name(s): linoleate dioxygenase, manganese lipoxygenase

Systematic name: linoleate:oxygen 11S-oxidoreductase

Comments: The product (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate, is converted, more slowly, into (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate. The enzyme from the fungus Gaeumannomyces graminis requires Mn2+. It also acts on α-linolenate, whereas γ-linolenate is a poor substrate. Oleate and arachidonate are not substrates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hamberg, M., Su, C. and Oliw, E.H. Manganese lipoxygenase: Discovery of bis-allylic hydroperoxide as product and intermediate in a lipoxygenase reaction. J. Biol. Chem. 273 (1998) 13080-13088. [PMID: 9582346]

2. Oliw, E.H., Su, C., Skogstrom, T. and Benthin, G. Analysis of novel hydroperoxides and other metabolites of oleic, linoleic, and linolenic acids by liquid chromatography-mass spectrometry with ion trap MSn. Lipids 33 (1998) 843-852. [PMID: 9778131]

3. Su, C. and Oliw, E.H. Manganese lipoxygenase: Purification and characterization. J. Biol. Chem. 273 (1998) 13072-13079. [PMID: 9582345]

[EC 1.13.11.45 created 2000]

EC 1.13.11.46

Accepted name: 4-hydroxymandelate synthase

Reaction: 4-hydroxyphenylpyruvate + O2 = (S)-4-hydroxymandelate + CO2

For diagram of reaction click here.

Glossary: (S)-4-hydroxymandelate = (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate

Other name(s): 4-hydroxyphenylpyruvate dioxygenase II

Systematic name: (S)-4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating)

Comments: Requires Fe2+. Involved in the biosynthesis of the vancomycin group of glycopeptide antibiotics.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 280566-04-3

References:

1. Hubbard, B.K., Thomas, M.G. and Walsh, C.T. Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics. Chem. Biol. 7 (2000) 931-942. [PMID: 11137816]

2. Choroba, O.W., Williams, D.H. and Spencer, J.B. Biosynthesis of the vancomycin group of antibiotics: involvement of an unusual dioxygenase in the pathway to (S)-4-hydroxyphenylglycine. J. Am. Chem. Soc. 122 (2000) 5389-5390.

[EC 1.13.11.46 created 2001]

EC 1.13.11.47

Accepted name: 3-hydroxy-4-oxoquinoline 2,4-dioxygenase

Reaction: 3-hydroxy-1H-quinolin-4-one + O2 = N-formylanthranilate + CO

For diagram click here.

Other name(s): (1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase; 3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase; 3-hydroxy-4(1H)-one, 2,4-dioxygenase; quinoline-3,4-diol 2,4-dioxygenase

Systematic name: 3-hydroxy-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)

Comments: Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Pseudomonas putida is highly specific for this substrate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 238093-32-8

References:

1. Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F. A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline. FEMS Microbiol. Lett. 117 (1994) 299-304.

2. Bauer, I., Max, N., Fetzner, S. and Lingens, F. 2,4-Dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1. Eur. J. Biochem. 240 (1996) 576-583. [PMID: 8856057]

3. Fischer, F., Kunne, S. and Fetzner, S. Bacterial 2,4-dioxygenases: new members of the α/β hydrolase-fold superfamily of enzymes functionally related to serine hydrolases. J. Bacteriol. 181 (1999) 5725-5733. [PMID: 10482514]

[EC 1.13.11.47 created 1999 as EC 1.13.99.5, transferred 2001 to EC 1.13.11.47 (EC 1.12.99.5 created 1999 deleted 2001 as identical)]

EC 1.13.11.48

Accepted name: 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase

Reaction: 3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO

For diagram click here.

Other name(s): (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase

Systematic name: 3-hydroxy-2-methyl-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)

Comments: Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Arthrobacter sp. can also act on 3-hydroxy-4-oxoquinoline, forming N-formylanthranilate and CO (cf. EC 1.13.11.47, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase), but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 160995-63-1

References:

1. Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F. A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline. FEMS Microbiol. Lett. 117 (1994) 299-304.

2. Bauer, I., Max, N., Fetzner, S. and Lingens, F. 2,4-Dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1. Eur. J. Biochem. 240 (1996) 576-583. [PMID: 8856057]

3. Fischer, F., Kunne, S. and Fetzner, S. Bacterial 2,4-dioxygenases: new members of the α/β hydrolase-fold superfamily of enzymes functionally related to serine hydrolases. J. Bacteriol. 181 (1999) 5725-5733. [PMID: 10482514]

[EC 1.13.11.48 created 2001]

EC 1.13.11.49

Accepted name: chlorite O2-lyase

Reaction: chloride + O2 = chlorite

Other name(s): [chlorite dismutase]

Systematic name: chloride:oxygen oxidoreductase

Comments: Reaction occurs in the reverse direction in chlorate- and perchlorate-reducing bacteria. There is no activity when chlorite is replaced by hydrogen peroxide, perchlorate, chlorate or nitrite. The term 'chlorite dismutase' is misleading as the reaction does not involve dismutation/disproportionation. Contains iron and protoheme IX.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number:

References:

1. van Ginkel, C.G., Rikken, G.B., Kron, A.G.M. and Kengen, S.W.M. Purification and characterization of chlorite dismutase: a novel oxygen-generating enzyme. Arch. Microbiol. 166 (1996) 321-326. [PMID: 8929278]

2. Stenklo, K., Thorell, H.D., Bergius, H., Aasa, R. and Nilsson, T. Chlorite dismutase from Ideonella dechloratans. J. Biol. Inorg. Chem. 6 (2001) 601-607. [PMID: 11472023]

[EC 1.13.11.49 created 2001]

EC 1.13.11.50

Accepted name: acetylacetone-cleaving enzyme

Reaction: pentane-2,4-dione + O2 = acetate + methylglyoxal

Glossary: methylglyoxal = 2-oxopropanal

Other name(s): Dke1; acetylacetone dioxygenase; diketone cleaving dioxygenase; diketone cleaving enzyme

Systematic name: acetylacetone:oxygen oxidoreductase

Comments: An Fe(II)-dependent enzyme. Forms the first step in the acetylacetone degradation pathway of Acinetobacter johnsonii. While acetylacetone is by far the best substrate, heptane-3,5-dione, octane-2,4-dione, 2-acetylcyclohexanone and ethyl acetoacetate can also act as substrates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 524047-53-8

References:

1. Straganz, G.D., Glieder, A., Brecker, L., Ribbons, D.W. and Steiner, W. Acetylacetone-cleaving enzyme Dke1: a novel C-C-bond-cleaving enzyme from Acinetobacter johnsonii. Biochem. J. 369 (2003) 573-581. [PMID: 12379146]

[EC 1.13.11.50 created 2003]

EC 1.13.11.51

Accepted name: 9-cis-epoxycarotenoid dioxygenase

Reaction: (1) a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal

(2) 9-cis-violaxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12'-apo-β-caroten-12'-al

(3) 9'-cis-neoxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6R)-3,5-dihydroxy-6,7-didehydro-5,6-dihydro-12'-apo-β-caroten-12'-al

For diagram click here.

Other name(s): nine-cis-epoxycarotenoid dioxygenase; NCED; AtNCED3; PvNCED1; VP14

Systematic name: 9-cis-epoxycarotenoid 11,12-dioxygenase

Comments: Requires iron(II). Acts on 9-cis-violaxanthin and 9'-cis-neoxanthin but not on the all-trans isomers [2,3]. In vitro, it will cleave 9-cis-zeaxanthin. Catalyses the first step of abscisic-acid biosynthesis from carotenoids in chloroplasts, in response to water stress. The other enzymes involved in the abscisic-acid biosynthesis pathway are EC 1.1.1.288 (xanthoxin dehydrogenase), EC 1.2.3.14 (abscisic aldehyde oxidase) and EC 1.14.13.93 [(+)-abscisic acid 8'-hydroxylase].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 199877-10-6

References:

1. Schwartz, S.H., Tan, B.C., Gage, D.A., Zeevaart, J.A. and McCarty, D.R. Specific oxidative cleavage of carotenoids by VP14 of maize. Science 276 (1997) 1872-1874. [PMID: 9188535]

2. Tan, B.C., Schwartz, S.H., Zeevaart, J.A. and McCarty, D.R. Genetic control of abscisic acid biosynthesis in maize. Proc. Natl. Acad. Sci. USA 94 (1997) 12235-12240. [PMID: 9342392]

3. Qin, X. and Zeevaart, J.A. The 9-cis-epoxycarotenoid cleavage reaction is the key regulatory step of abscisic acid biosynthesis in water-stressed bean. Proc. Natl. Acad. Sci. USA 96 (1999) 15354-15361. [PMID: 10611388]

4. Thompson, A.J., Jackson, A.C., Symonds, R.C., Mulholland, B.J., Dadswell, A.R., Blake, P.S., Burbidge, A. and Taylor, I.B. Ectopic expression of a tomato 9-cis-epoxycarotenoid dioxygenase gene causes over-production of abscisic acid. Plant J. 23 (2000) 363-374. [PMID: 10929129]

5. Iuchi, S., Kobayashi, M., Taji, T., Naramoto, M., Seki, M., Kato, T., Tabata, S., Kakubari, Y., Yamaguchi-Shinozaki, K. and Shinozaki, K. Regulation of drought tolerance by gene manipulation of 9-cis-epoxycarotenoid dioxygenase, a key enzyme in abscisic acid biosynthesis in Arabidopsis. Plant J. 27 (2001) 325-333. [PMID: 11532178]

6. Iuchi, S., Kobayashi, M., Taji, T., Naramoto, M., Seki, M., Kato, T., Tabata, S., Kakubari, Y., Yamaguchi-Shinozaki, K. and Shinozaki, K. Regulation of drought tolerance by gene manipulation of 9-cis-epoxycarotenoid dioxygenase, a key enzyme in abscisic acid biosynthesis in Arabidopsis. Erratum. Plant J. 30 (2002) 611. [PMID: 11532178]

[EC 1.13.11.51 created 2005]

EC 1.13.11.52

Accepted name: indoleamine 2,3-dioxygenase

Reaction: (1) D-tryptophan + O2 = N-formyl-D-kynurenine

(2) L-tryptophan + O2 = N-formyl-L-kynurenine

For diagram, click here

Other name(s): IDO (ambiguous); tryptophan pyrrolase (ambiguous); D-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)

Systematic name: D-tryptophan:oxygen 2,3-oxidoreductase (ring-opening)

Comments: A protohemoprotein. Requires ascorbic acid and methylene blue for activity. This enzyme has broader substrate specificity than EC 1.13.11.11, tryptophan 2,3-dioxygenase [1]. It is induced in response to pathological conditions and host-defense mechanisms and its distribution in mammals is not confined to the liver [2]. While the enzyme is more active with D-tryptophan than L-tryptophan, its only known function to date is in the metabolism of L-tryptophan [2,6]. Superoxide radicals can replace O2 as oxygen donor [4,7].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9014-51-1

References:

1. Yamamoto, S. and Hayaishi, O. Tryptophan pyrrolase of rabbit intestine. D- and L-tryptophan-cleaving enzyme or enzymes. J. Biol. Chem. 242 (1967) 5260-5266. [PMID: 6065097]

2. Yasui, H., Takai, K., Yoshida, R. and Hayaishi, O. Interferon enhances tryptophan metabolism by inducing pulmonary indoleamine 2,3-dioxygenase: its possible occurrence in cancer patients. Proc. Natl. Acad. Sci. USA 83 (1986) 6622-6626. [PMID: 2428037]

3. Takikawa, O., Yoshida, R., Kido, R. and Hayaishi, O. Tryptophan degradation in mice initiated by indoleamine 2,3-dioxygenase. J. Biol. Chem. 261 (1986) 3648-3653. [PMID: 2419335]

4. Hirata, F., Ohnishi, T. and Hayaishi, O. Indoleamine 2,3-dioxygenase. Characterization and properties of enzyme. O2- complex. J. Biol. Chem. 252 (1977) 4637-4642. [PMID: 194886]

5. Dang, Y., Dale, W.E. and Brown, O.R. Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway. Free Radic. Biol. Med. 28 (2000) 615-624. [PMID: 10719243]

6. Littlejohn, T.K., Takikawa, O., Truscott, R.J. and Walker, M.J. Asp274 and His346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase. J. Biol. Chem. 278 (2003) 29525-29531. [PMID: 12766158]

7. Thomas, S.R. and Stocker, R. Redox reactions related to indoleamine 2,3-dioxygenase and tryptophan metabolism along the kynurenine pathway. Redox Rep. 4 (1999) 199-220. [PMID: 10731095]

8. Sono, M. Spectroscopic and equilibrium studies of ligand and organic substrate binding to indolamine 2,3-dioxygenase. Biochemistry 29 (1990) 1451-1460. [PMID: 2334706]

[EC 1.13.11.52 created 2006]

EC 1.13.11.53

Accepted name: acireductone dioxygenase (Ni2+-requiring)

Reaction: 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate + CO

For diagram click here or mechanism click here

Other name(s): ARD; 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous); acireductone dioxygenase (ambiguous); E-2

Systematic name: 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate- and CO-forming)

Comments: Requires Ni2+. If iron(II) is bound instead of Ni2+, the reaction catalysed by EC 1.13.11.54, acireductone dioxygenase [iron(II)-requiring], occurs instead [1]. The enzyme from Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Wray, J.W. and Abeles, R.H. A bacterial enzyme that catalyzes formation of carbon monoxide. J. Biol. Chem. 268 (1993) 21466-21469. [PMID: 8407993]

2. Wray, J.W. and Abeles, R.H. The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J. Biol. Chem. 270 (1995) 3147-3153. [PMID: 7852397]

3. Furfine, E.S. and Abeles, R.H. Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae. J. Biol. Chem. 263 (1988) 9598-9606. [PMID: 2838472]

4. Dai, Y., Wensink, P.C. and Abeles, R.H. One protein, two enzymes. J. Biol. Chem. 274 (1999) 1193-1195. [PMID: 9880484]

5. Mo, H., Dai, Y., Pochapsky, S.S. and Pochapsky, T.C. 1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae. J. Biomol. NMR 14 (1999) 287-288. [PMID: 10481280]

6. Dai, Y., Pochapsky, T.C. and Abeles, R.H. Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae. Biochemistry 40 (2001) 6379-6387. [PMID: 11371200]

7. Al-Mjeni, F., Ju, T., Pochapsky, T.C. and Maroney, M.J. XAS investigation of the structure and function of Ni in acireductone dioxygenase. Biochemistry 41 (2002) 6761-6769. [PMID: 12022880]

8. Pochapsky, T.C., Pochapsky, S.S., Ju, T., Mo, H., Al-Mjeni, F. and Maroney, M.J. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol. 9 (2002) 966-972. [PMID: 12402029]

[EC 1.13.11.53 created 2006]

EC 1.13.11.54

Accepted name: acireductone dioxygenase [iron(II)-requiring]

Reaction: 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 4-(methylthio)-2-oxobutanoate + formate

For diagram click here or mechanism click here

Other name(s): ARD'; 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous); acireductone dioxygenase (ambiguous); E-2'

Systematic name: 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate-forming)

Comments: Requires iron(II). If Ni2+ is bound instead of iron(II), the reaction catalysed by EC 1.13.11.53, acireductone dioxygenase (Ni2+-requiring), occurs instead. The enzyme from Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Wray, J.W. and Abeles, R.H. A bacterial enzyme that catalyzes formation of carbon monoxide. J. Biol. Chem. 268 (1993) 21466-21469. [PMID: 8407993]

2. Wray, J.W. and Abeles, R.H. The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J. Biol. Chem. 270 (1995) 3147-3153. [PMID: 7852397]

3. Furfine, E.S. and Abeles, R.H. Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae. J. Biol. Chem. 263 (1988) 9598-9606. [PMID: 2838472]

4. Dai, Y., Wensink, P.C. and Abeles, R.H. One protein, two enzymes. J. Biol. Chem. 274 (1999) 1193-1195. [PMID: 9880484]

5. Mo, H., Dai, Y., Pochapsky, S.S. and Pochapsky, T.C. 1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae. J. Biomol. NMR 14 (1999) 287-288. [PMID: 10481280]

6. Dai, Y., Pochapsky, T.C. and Abeles, R.H. Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae. Biochemistry 40 (2001) 6379-6387. [PMID: 11371200]

7. Al-Mjeni, F., Ju, T., Pochapsky, T.C. and Maroney, M.J. XAS investigation of the structure and function of Ni in acireductone dioxygenase. Biochemistry 41 (2002) 6761-6769. [PMID: 12022880]

8. Pochapsky, T.C., Pochapsky, S.S., Ju, T., Mo, H., Al-Mjeni, F. and Maroney, M.J. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol. 9 (2002) 966-972. [PMID: 12402029]

[EC 1.13.11.54 created 2006]

EC 1.13.11.55

Accepted name: sulfur oxygenase/reductase

Reaction: 4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 HSO3 + 2 H+

Glossary: bisulfite = HSO3

Other name(s): SOR; sulfur oxygenase; sulfur oxygenase reductase

Systematic name: sulfur:oxygen oxidoreductase (hydrogen-sulfide- and sulfite-forming)

Comments: This enzyme, which is found in thermophilic microorganisms, contains one mononuclear none-heme iron centre per subunit. Elemental sulfur is both the electron donor and one of the two known acceptors, the other being oxygen. Another reaction product is thiosulfate, but this is probably formed non-enzymically at elevated temperature from sulfite and sulfur [1]. This enzyme differs from EC 1.13.11.18, sulfur dioxygenase and EC 1.12.98.4, sulfur reductase, in that both activities are found together.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 120598-92-7

References:

1. Kletzin, A. Coupled enzymatic production of sulfite, thiosulfate, and hydrogen sulfide from sulfur: purification and properties of a sulfur oxygenase reductase from the facultatively anaerobic archaebacterium Desulfurolobus ambivalens. J. Bacteriol. 171 (1989) 1638-1643. [PMID: 2493451]

2. Kletzin, A. Molecular characterization of the sor gene, which encodes the sulfur oxygenase/reductase of the thermoacidophilic Archaeum Desulfurolobus ambivalens. J. Bacteriol. 174 (1992) 5854-5859. [PMID: 1522063]

3. Sun, C.W., Chen, Z.W., He, Z.G., Zhou, P.J. and Liu, S.J. Purification and properties of the sulfur oxygenase/reductase from the acidothermophilic archaeon, Acidianus strain S5. Extremophiles 7 (2003) 131-134. [PMID: 12664265]

4. Urich, T., Bandeiras, T.M., Leal, S.S., Rachel, R., Albrecht, T., Zimmermann, P., Scholz, C., Teixeira, M., Gomes, C.M. and Kletzin, A. The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre. Biochem. J. 381 (2004) 137-146. [PMID: 15030315]

[EC 1.13.11.55 created 2006]

EC 1.13.11.56

Accepted name: 1,2-dihydroxynaphthalene dioxygenase

Reaction: naphthalene-1,2-diol + O2 = 2-hydroxy-2H-chromene-2-carboxylate

For diagram of reaction, click here

Other name(s): 1,2-DHN dioxygenase; DHNDO; 1,2-dihydroxynaphthalene oxygenase; 1,2-dihydroxynaphthalene:oxygen oxidoreductase

Systematic name: naphthalene-1,2-diol:oxygen oxidoreductase

Comments: This enzyme is involved in naphthalene degradation. Requires Fe2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:

References:

1. Kuhm, A.E., Stolz, A., Ngai, K.L. and Knackmuss, H.J. Purification and characterization of a 1,2-dihydroxynaphthalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids. J. Bacteriol. 173 (1991) 3795-3802. [PMID: 2050635]

2. Keck, A., Conradt, D., Mahler, A., Stolz, A., Mattes, R. and Klein, J. Identification and functional analysis of the genes for naphthalenesulfonate catabolism by Sphingomonas xenophaga BN6. Microbiology 152 (2006) 1929-1940. [PMID: 16804169]

3. Patel, T.R. and Barnsley, E.A. Naphthalene metabolism by pseudomonads: purification and properties of 1,2-dihydroxynaphthalene oxygenase. J. Bacteriol. 143 (1980) 668-673. [PMID: 7204331]

[EC 1.13.11.56 created 2010]

EC 1.13.11.57

Accepted name: gallate dioxygenase

Reaction: gallate + O2 = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate

For diagram of reaction click here

Other name(s): GalA

Systematic name: gallate:oxygen oxidoreductase

Comments: Contains non-heme Fe2+. The enzyme is a ring-cleavage dioxygenase that acts specifically on gallate to produce the keto-tautomer of 4-oxalomesaconate [1,2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:

References:

1. Nogales, J., Canales, A., JimŽnez-Barbero, J., García, J.L. and Díaz, E. Molecular characterization of the gallate dioxygenase from Pseudomonas putida KT2440. The prototype of a new subgroup of extradiol dioxygenases. J. Biol. Chem. 280 (2005) 35382-35390. [PMID: 16030014]

2. Nogales, J., Canales, A., Jimenez-Barbero, J., Serra, B., Pingarron, J.M., Garcia, J.L. and Diaz, E. Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida. Mol. Microbiol. 79 (2011) 359-374. [PMID: 21219457]

[EC 1.13.11.57 created 2011]

EC 1.13.11.58

Accepted name: linoleate 9S-lipoxygenase

Reaction: linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate

Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate

Other name(s): 9-lipoxygenase; 9S-lipoxygenase; linoleate 9-lipoxygenase; LOX1 (gene name); 9S-LOX

Systematic name: linoleate:oxygen 9S-oxidoreductase

Comments: Contains nonheme iron. A common plant lipoxygenase that oxidizes linoleate and α-linolenate, the two most common polyunsaturated fatty acids in plants, by inserting molecular oxygen at the C9 position with (S)-configuration. The enzyme plays a physiological role during the early stages of seedling growth. The enzyme from Arabidopsis thaliana shows comparable activity towards linoleate and linolenate [4]. EC 1.13.11.12 (linoleate 13S-lipoxygenase) catalyses a similar reaction at another position of these fatty acids.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Vellosillo, T., Martinez, M., Lopez, M.A., Vicente, J., Cascon, T., Dolan, L., Hamberg, M. and Castresana, C. Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade. Plant Cell 19 (2007) 831-846. [PMID: 17369372]

2. Boeglin, W.E., Itoh, A., Zheng, Y., Coffa, G., Howe, G.A. and Brash, A.R. Investigation of substrate binding and product stereochemistry issues in two linoleate 9-lipoxygenases. Lipids 43 (2008) 979-987. [PMID: 18795358]

3. Andreou, A.Z., Hornung, E., Kunze, S., Rosahl, S. and Feussner, I. On the substrate binding of linoleate 9-lipoxygenases. Lipids 44 (2009) 207-215. [PMID: 19037675]

4. Bannenberg, G., Martinez, M., Hamberg, M. and Castresana, C. Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana. Lipids 44 (2009) 85-95. [PMID: 18949503]

[EC 1.13.11.58 created 2011]

EC 1.13.11.59

Accepted name: torulene dioxygenase

Reaction: torulene + O2 = 4'-apo-β,ψ-caroten-4'-al + 3-methylbut-2-enal

For diagram of reaction click here

Glossary: torulene = 3',4'-didehydro-β,ψ-carotene

Other name(s): CAO-2; CarT

Systematic name: torulene:oxygen oxidoreductase

Comments: It is assumed that 3-methylbut-2-enal is formed. The enzyme cannot cleave the saturated 3',4'-bond of γ-carotene which implies that a 3',4'-double bond is neccessary for this reaction.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Prado-Cabrero, A., Estrada, A.F., Al-Babili, S. and Avalos, J. Identification and biochemical characterization of a novel carotenoid oxygenase: elucidation of the cleavage step in the Fusarium carotenoid pathway. Mol. Microbiol. 64 (2007) 448-460. [PMID: 17493127]

2. Saelices, L., Youssar, L., Holdermann, I., Al-Babili, S. and Avalos, J. Identification of the gene responsible for torulene cleavage in the Neurospora carotenoid pathway. Mol. Genet. Genomics 278 (2007) 527-537. [PMID: 17610084]

3. Estrada, A.F., Maier, D., Scherzinger, D., Avalos, J. and Al-Babili, S. Novel apocarotenoid intermediates in Neurospora crassa mutants imply a new biosynthetic reaction sequence leading to neurosporaxanthin formation. Fungal Genet. Biol. 45 (2008) 1497-1505. [PMID: 18812228]

[EC 1.13.11.59 created 2011]

EC 1.13.11.60

Accepted name: linoleate 8R-lipoxygenase

Reaction: linoleate + O2 = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate

Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate

Other name(s): linoleic acid 8R-dioxygenase; 5,8-LDS (bifunctional enzyme); 7,8-LDS (bifunctional enzyme); 5,8-linoleate diol synthase (bifunctional enzyme); 7,8-linoleate diol synthase (bifunktional enzyme); PpoA

Systematic name: linoleate:oxygen (8R)-oxidoreductase

Comments: The enzyme contains heme [1,4]. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5, 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase) [1]. The bifunctional enzyme from Gaeumannomyces graminis also catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase) [4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Brodhun, F., Gobel, C., Hornung, E. and Feussner, I. Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450. J. Biol. Chem. 284 (2009) 11792-11805. [PMID: 19286665]

2. Hamberg, M., Zhang, L.-Y., Brodowsky, I.D. and Oliw, E.H. Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces graminis: stereochemistry of dioxygenase and hydroperoxide isomerase reactions. Arch. Biochem. Biophys. 309 (1994) 77-80. [PMID: 8117115]

3. Garscha, U. and Oliw, E. Pichia expression and mutagenesis of 7,8-linoleate diol synthase change the dioxygenase and hydroperoxide isomerase. Biochem. Biophys. Res. Commun. 373 (2008) 579-583. [PMID: 18586008]

4. Su, C. and Oliw, E.H. Purification and characterization of linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein. J. Biol. Chem. 271 (1996) 14112-14118. [PMID: 8662736]

[EC 1.13.11.60 created 2011]

EC 1.13.11.61

Accepted name: linolenate 9R-lipoxygenase

Reaction: α-linolenate + O2 = (9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate

Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate
α-linolenate = (9Z,12Z,15Z)-octadeca-9,12,15-trienoate

Other name(s): NspLOX; (9R)-LOX; linoleate 9R-dioxygenase

Systematic name: α-linolenate:oxygen (9R)-oxidoreductase

Comments: In cyanobacteria the enzyme is involved in oxylipin biosynthesis. The enzyme also converts linoleate to (9R,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Jerneren, F., Hoffmann, I. and Oliw, E.H. Linoleate 9R-dioxygenase and allene oxide synthase activities of Aspergillus terreus. Arch. Biochem. Biophys. 495 (2010) 67-73. [PMID: 20043865]

2. Andreou, A.Z., Vanko, M., Bezakova, L. and Feussner, I. Properties of a mini 9R-lipoxygenase from Nostoc sp. PCC 7120 and its mutant forms. Phytochemistry 69 (2008) 1832-1837. [PMID: 18439634]

3. Lang, I., Gobel, C., Porzel, A., Heilmann, I. and Feussner, I. A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120. Biochem. J. 410 (2008) 347-357. [PMID: 18031288]

[EC 1.13.11.61 created 2011]

EC 1.13.11.62

Accepted name: linoleate 10R-lipoxygenase

Reaction: linoleate + O2 = (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate

Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate

Other name(s): 10R-DOX; (10R)-dioxygenase; 10R-dioxygenase

Systematic name: linoleate:oxygen (10R)-oxidoreductase

Comments: The enzyme is involved in biosynthesis of oxylipins, which affect sporulation, development, and pathogenicity of Aspergillus spp.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Garscha, U. and Oliw, E.H. Leucine/valine residues direct oxygenation of linoleic acid by (10R)- and (8R)-dioxygenases: expression and site-directed mutagenesis of (10R)-dioxygenase with epoxyalcohol synthase activity. J. Biol. Chem. 284 (2009) 13755-13765. [PMID: 19289462]

2. Jerneren, F., Garscha, U., Hoffmann, I., Hamberg, M. and Oliw, E.H. Reaction mechanism of 5,8-linoleate diol synthase, 10R-dioxygenase, and 8,11-hydroperoxide isomerase of Aspergillus clavatus. Biochim. Biophys. Acta 1801 (2010) 503-507. [PMID: 20045744]

[EC 1.13.11.62 created 2011]

EC 1.13.11.63

Accepted name: β-carotene 15,15'-dioxygenase

Reaction: β-carotene + O2 = 2 all-trans-retinal

For diagram of reaction click here.

Other name(s): blh (gene name); BCO1 (gene name); BCDO (gene name); carotene dioxygenase; carotene 15,15'-dioxygenase; BCMO1 (misleading); β-carotene 15,15'-monooxygenase (incorrect)

Systematic name: β-carotene:oxygen 15,15'-dioxygenase (bond-cleaving)

Comments: Requires Fe2+. The enzyme cleaves β-carotene symmetrically, producing two molecules of all-trans-retinal. Both atoms of the oxygen molecule are incorporated into the products [8]. The enzyme can also process β-cryptoxanthin, 8'-apo-β-carotenal, 4'-apo-β-carotenal, α-carotene and γ-carotene in decreasing order. The presence of at least one unsubstituted β-ionone ring in a substrate greater than C30 is mandatory [5]. A prokaryotic enzyme has been reported from the uncultured marine bacterium 66A03, where it is involved in the proteorhodopsin system, which uses retinal as its chromophore [6,7].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Goodman, D.S., Huang, H.S. and Shiratori, T. Mechanism of the biosynthesis of vitamin A from β-carotene. J. Biol. Chem. 241 (1966) 1929-1932. [PMID: 5946623]

2. Goodman, D.S., Huang, H.S., Kanai, M. and Shiratori, T. The enzymatic conversion of all-trans β-carotene into retinal. J. Biol. Chem. 242 (1967) 3543-3554.

3. Yan, W., Jang, G.F., Haeseleer, F., Esumi, N., Chang, J., Kerrigan, M., Campochiaro, M., Campochiaro, P., Palczewski, K. and Zack, D.J. Cloning and characterization of a human β,β-carotene-15,15'-dioxygenase that is highly expressed in the retinal pigment epithelium. Genomics 72 (2001) 193-202. [PMID: 11401432]

4. Leuenberger, M.G., Engeloch-Jarret, C. and Woggon, W.D. The reaction mechanism of the enzyme-catalysed central cleavage of β-carotene to retinal. Angew. Chem. 40 (2001) 2614-2616. [PMID: 11458349]

5. Kim, Y.S. and Oh, D.K. Substrate specificity of a recombinant chicken β-carotene 15,15'-monooxygenase that converts β-carotene into retinal. Biotechnol. Lett. 31 (2009) 403-408. [PMID: 18979213]

6. Kim, Y.S., Kim, N.H., Yeom, S.J., Kim, S.W. and Oh, D.K. In vitro characterization of a recombinant Blh protein from an uncultured marine bacterium as a β-carotene 15,15'-dioxygenase. J. Biol. Chem. 284 (2009) 15781-15793. [PMID: 19366683]

7. Kim, Y.S., Park, C.S. and Oh, D.K. Retinal production from β-carotene by β-carotene 15,15'-dioxygenase from an unculturable marine bacterium. Biotechnol. Lett. 32 (2010) 957-961. [PMID: 20229064]

8. dela Seña, C., Riedl, K.M., Narayanasamy, S., Curley, R.W., Jr., Schwartz, S.J. and Harrison, E.H. The human enzyme that converts dietary provitamin A carotenoids to vitamin A is a dioxygenase. J. Biol. Chem. 289 (2014) 13661-13666. [PMID: 24668807]

[EC 1.13.11.63 created 2012 (EC 1.14.99.36 created 1972 as EC 1.13.11.21, transferred 2001 to EC 1.14.99.36, incorporated 2015), modified 2016]

EC 1.13.11.64

Accepted name: 5-nitrosalicylate dioxygenase

Reaction: 5-nitrosalicylate + O2 = 2-oxo-3-(5-oxofuran-2-ylidene)propanoate + nitrite (overall reaction)
(1a) 5-nitrosalicylate + O2 = 4-nitro-6-oxohepta-2,4-dienedioate
(1b) 4-nitro-6-oxohepta-2,4-dienedioate = 2-oxo-3-(5-oxofuran-2-ylidene)propanoate + nitrite (spontaneous)

Other name(s): naaB (gene name); 5-nitrosalicylate:oxygen 1,2-oxidoreductase (decyclizing)

Systematic name: 5-nitrosalicylate:oxygen 1,2-oxidoreductase (ring-opening)

Comments: The enzyme, characterized from the soil bacterium Bradyrhizobium sp. JS329, is involved in the pathway of 5-nitroanthranilate degradation. It is unusual in being able to catalyse the ring fission without the requirement for prior removal of the nitro group. The product undergoes spontaneous lactonization, with concurrent elimination of the nitro group.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:

References:

1. Qu, Y. and Spain, J.C. Biodegradation of 5-nitroanthranilic acid by Bradyrhizobium sp. strain JS329. Appl. Environ. Microbiol. 76 (2010) 1417-1422. [PMID: 20081004]

2. Qu, Y. and Spain, J.C. Molecular and biochemical characterization of the 5-nitroanthranilic acid degradation pathway in Bradyrhizobium sp. strain JS329. J. Bacteriol. 193 (2011) 3057-3063. [PMID: 21498645]

[EC 1.13.11.64 created 2012]

EC 1.13.11.65

Accepted name: carotenoid isomerooxygenase

Reaction: zeaxanthin + O2 = (3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal

For diagram of reaction click here.

Other name(s): ninaB (gene name)

Systematic name: zeaxanthin:oxygen 15,15'-oxidoreductase (bond-cleaving, cis-isomerizing)

Comments: The enzyme, characterized from the moth Galleria mellonella and the fruit fly Drosophila melanogaster, is involved in the synthesis of retinal from dietary caroteoids in insects. The enzyme accepts different all-trans carotenoids, including β-carotene, α-carotene and lutein, and catalyses the symmetrical cleavage of the carotenoid and the simultaneous isomerization of only one of the products to a cis configuration. When the substrate is hydroxylated only in one side (as in cryptoxanthin), the enzyme preferentially isomerizes the hydroxylated part of the molecule.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Oberhauser, V., Voolstra, O., Bangert, A., von Lintig, J. and Vogt, K. NinaB combines carotenoid oxygenase and retinoid isomerase activity in a single polypeptide. Proc. Natl. Acad. Sci. USA 105 (2008) 19000-19005. [PMID: 19020100]

[EC 1.13.11.65 created 2012 as EC 1.14.13.164, transferred 2012 to EC 1.13.11.65]

EC 1.13.11.66

Accepted name: hydroquinone 1,2-dioxygenase

Reaction: benzene-1,4-diol + O2 = (2E,4Z)-4-hydroxy-6-oxohexa-2,4-dienoate

For diagram of reaction click here.

Glossary: benzene-1,4-diol = hydroquinone
(2E,4Z)-4-hydroxy-6-oxohexa-2,4-dienoate = 4-hydroxymuconic semialdehyde

Other name(s): hydroquinone dioxygenase; benzene-1,4-diol:oxygen 1,2-oxidoreductase (decyclizing)

Systematic name: benzene-1,4-diol:oxygen 1,2-oxidoreductase (ring-opening)

Comments: The enzyme is an extradiol-type dioxygenase, and is a member of the nonheme-iron(II)-dependent dioxygenase family. It catalyses the ring cleavage of a wide range of hydroquinone substrates to produce the corresponding 4-hydroxymuconic semialdehydes.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Miyauchi, K., Adachi, Y., Nagata, Y. and Takagi, M. Cloning and sequencing of a novel meta-cleavage dioxygenase gene whose product is involved in degradation of γ-hexachlorocyclohexane in Sphingomonas paucimobilis. J. Bacteriol. 181 (1999) 6712-6719. [PMID: 10542173]

2. Moonen, M.J., Synowsky, S.A., van den Berg, W.A., Westphal, A.H., Heck, A.J., van den Heuvel, R.H., Fraaije, M.W. and van Berkel, W.J. Hydroquinone dioxygenase from pseudomonas fluorescens ACB: a novel member of the family of nonheme-iron(II)-dependent dioxygenases. J. Bacteriol. 190 (2008) 5199-5209. [PMID: 18502867]

3. Shen, W., Liu, W., Zhang, J., Tao, J., Deng, H., Cao, H. and Cui, Z. Cloning and characterization of a gene cluster involved in the catabolism of p-nitrophenol from Pseudomonas putida DLL-E4. Bioresour. Technol. 101 (2010) 7516-7522. [PMID: 20466541]

[EC 1.13.11.66 created 2012]

EC 1.13.11.67

Accepted name: 8'-apo-β-carotenoid 14',13'-cleaving dioxygenase

Reaction: 8'-apo-β-carotenol + O2 = 14'-apo-β-carotenal + an uncharacterized product

For diagram of reaction click here.

Other names: 8'-apo-β-carotenol:O2 oxidoreductase (14',13'-cleaving)

Systematic name(s): 8'-apo-β-carotenol:oxygen oxidoreductase (14',13'-cleaving)

Comments: A thiol-dependent enzyme isolated from rat and rabbit. Unlike EC 1.13.11.63, β-carotene-15,15'-monooxygenase, it is not active towards β-carotene. The secondary product has not been characterized, but may be (3E,5E)-7-hydroxy-6-methylhepta-3,5-dien-2-one.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 198028-39-6

References:

1. Dmitrovskii, A.A., Gessler, N.N., Gomboeva, S.B., Ershov, Yu.V. and Bykhovsky, V.Ya. Enzymatic oxidation of β-apo-8'-carotenol to β-apo-14'-carotenal by an enzyme different from β-carotene-15,15'-dioxygenase. Biochemistry (Mosc) 62 (1997) 787-792. [PMID: 9331970]

[EC 1.13.11.67 created 2000 as EC 1.13.12.12, transferred 2012 to EC 1.13.11.67]

EC 1.13.11.68

Accepted name: 9-cis-β-carotene 9',10'-cleaving dioxygenase

Reaction: 9-cis-β-carotene + O2 = 9-cis-10'-apo-β-carotenal + β-ionone

For diagram of reaction click here.

Glossary: β-ionone = (3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-one

Other name(s): CCD7 (gene name); MAX3 (gene name); NCED7 (gene name); 9-cis-β-carotene:O2 oxidoreductase (9',10'-cleaving)

Systematic name: 9-cis-β-carotene:oxygen oxidoreductase (9',10'-cleaving)

Comments: Requires Fe2+. The enzyme participates in a pathway leading to biosynthesis of strigolactones, plant hormones involved in promotion of symbiotic associations known as arbuscular mycorrhiza.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Booker, J., Auldridge, M., Wills, S., McCarty, D., Klee, H. and Leyser, O. MAX3/CCD7 is a carotenoid cleavage dioxygenase required for the synthesis of a novel plant signaling molecule. Curr. Biol. 14 (2004) 1232-1238. [PMID: 15268852]

2. Alder, A., Jamil, M., Marzorati, M., Bruno, M., Vermathen, M., Bigler, P., Ghisla, S., Bouwmeester, H., Beyer, P. and Al-Babili, S. The path from β-carotene to carlactone, a strigolactone-like plant hormone. Science 335 (2012) 1348-1351. [PMID: 22422982]

[EC 1.13.11.68 created 2012]

EC 1.13.11.69

Accepted name: carlactone synthase

Reaction: 9-cis-10'-apo-β-carotenal + 2 O2 = carlactone + (2E,4E,6E)-7-hydroxy-4-methylhepta-2,4,6-trienal

For diagram of reaction click here and mechanism click here.

Glossary: carlactone = 3-methyl-5-{[(1Z,3E)-2-methyl-4-(2,6,6-trimethylcyclohex-1-en-1-yl)buta-1,3-dien-1-yl]oxy}-5H-furan-2-one

Other name(s): CCD8 (gene name); MAX4 (gene name); NCED8 (gene name); 9-cis-10'-apo-β-carotenal:O2 oxidoreductase (14,15-cleaving, carlactone-forming)

Systematic name: 9-cis-10'-apo-β-carotenal:oxygen oxidoreductase (14,15-cleaving, carlactone-forming)

Comments: Requires Fe2+. The enzyme participates in a pathway leading to biosynthesis of strigolactones, plant hormones involved in promotion of symbiotic associations known as arbuscular mycorrhiza. Also catalyses EC 1.13.11.70, all-trans-10'-apo-β-carotenal 13,14-cleaving dioxygenase, but 10-fold slower. The secondary product has not been characterized, but may be (2E,4E,6E)-7-hydroxy-4-methylhepta-2,4,6-trienal or one of its tautomers. The preferred tautomeric form is not known.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Sorefan, K., Booker, J., Haurogne, K., Goussot, M., Bainbridge, K., Foo, E., Chatfield, S., Ward, S., Beveridge, C., Rameau, C. and Leyser, O. MAX4 and RMS1 are orthologous dioxygenase-like genes that regulate shoot branching in Arabidopsis and pea. Genes Dev. 17 (2003) 1469-1474. [PMID: 12815068]

2. Schwartz, S.H., Qin, X. and Loewen, M.C. The biochemical characterization of two carotenoid cleavage enzymes from Arabidopsis indicates that a carotenoid-derived compound inhibits lateral branching. J. Biol. Chem. 279 (2004) 46940-46945. [PMID: 15342640]

3. Alder, A., Jamil, M., Marzorati, M., Bruno, M., Vermathen, M., Bigler, P., Ghisla, S., Bouwmeester, H., Beyer, P. and Al-Babili, S. The path from β-carotene to carlactone, a strigolactone-like plant hormone. Science 335 (2012) 1348-1351. [PMID: 22422982]

[EC 1.13.11.69 created 2012]

EC 1.13.11.70

Accepted name: all-trans-10'-apo-β-carotenal 13,14-cleaving dioxygenase

Reaction: all-trans-10'-apo-β-carotenal + O2 = 13-apo-β-carotenone + (2E,4E,6E)-4-methylocta-2,4,6-trienedial

For diagram of reaction click here.

Other name(s): CCD8 (gene name); MAX4 (gene name); NCED8 (gene name); all-trans-10'-apo-β-carotenal:O2 oxidoreductase (13,14-cleaving)

Systematic name: all-trans-10'-apo-β-carotenal:oxygen oxidoreductase (13,14-cleaving)

Comments: Requires Fe2+. The enzyme from the plant Arabidopsis thaliana also catalyses EC 1.13.11.69, carlactone synthase, 10-fold faster.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Schwartz, S.H., Qin, X. and Loewen, M.C. The biochemical characterization of two carotenoid cleavage enzymes from Arabidopsis indicates that a carotenoid-derived compound inhibits lateral branching. J. Biol. Chem. 279 (2004) 46940-46945. [PMID: 15342640]

[EC 1.13.11.70 created 2012]

EC 1.13.11.71

Accepted name: carotenoid-9',10'-cleaving dioxygenase

Reaction: all-trans-β-carotene + O2 = all-trans-10'-apo-β-carotenal + β-ionone

For diagram of reaction click here.

Other name(s): BCO2 (gene name); β-carotene 9',10'-monooxygenase (misleading); all-trans-β-carotene:O2 oxidoreductase (9',10'-cleaving)

Systematic name: all-trans-β-carotene:oxygen oxidoreductase (9',10'-cleaving)

Comments: Requires Fe2+. The enzyme catalyses the asymmetric oxidative cleavage of carotenoids. The mammalian enzyme can also cleave all-trans-lycopene.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kiefer, C., Hessel, S., Lampert, J.M., Vogt, K., Lederer, M.O., Breithaupt, D.E. and von Lintig, J. Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A. J. Biol. Chem. 276 (2001) 14110-14116. [PMID: 11278918]

2. Lindqvist, A., He, Y.G. and Andersson, S. Cell type-specific expression of β-carotene 9',10'-monooxygenase in human tissues. J. Histochem. Cytochem. 53 (2005) 1403-1412. [PMID: 15983114]

[EC 1.13.11.71 created 2012]

EC 1.13.11.72

Accepted name: 2-hydroxyethylphosphonate dioxygenase

Reaction: 2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate

For diagram of reaction click here.

Other name(s): HEPD; phpD (gene name); 2-hydroxyethylphosphonate:O2 1,2-oxidoreductase (hydroxymethylphosphonate forming)

Systematic name: 2-hydroxyethylphosphonate:oxygen1,2-oxidoreductase (hydroxymethylphosphonate forming)

Comments: Requires non-heme-Fe(II). Isolated from some bacteria including Streptomyces hygroscopicus and Streptomyces viridochromogenes. The pro-R hydrogen at C-2 of the ethyl group is retained by the formate ion. Any stereochemistry at C-1 of the ethyl group is lost. One atom from dioxygen is present in each product. Involved in phosphinothricin biosynthesis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Cicchillo, R.M., Zhang, H., Blodgett, J.A., Whitteck, J.T., Li, G., Nair, S.K., van der Donk, W.A. and Metcalf, W.W. An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis. Nature 459 (2009) 871-874. [PMID: 19516340]

2. Whitteck, J.T., Malova, P., Peck, S.C., Cicchillo, R.M., Hammerschmidt, F. and van der Donk, W.A. On the stereochemistry of 2-hydroxyethylphosphonate dioxygenase. J. Am. Chem. Soc. 133 (2011) 4236-4239. [PMID: 21381767]

3. Peck, S.C., Cooke, H.A., Cicchillo, R.M., Malova, P., Hammerschmidt, F., Nair, S.K. and van der Donk, W.A. Mechanism and substrate recognition of 2-hydroxyethylphosphonate dioxygenase. Biochemistry 50 (2011) 6598-6605. [PMID: 21711001]

[EC 1.13.11.72 created 2012]

EC 1.13.11.73

Accepted name: methylphosphonate synthase

Reaction: 2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3-

For diagram of reaction click here.

Systematic name: 2-hydroxyethylphosphonate:oxygen 1,2-oxidoreductase (methylphosphonate forming)

Comments: Isolated from the marine archaeon Nitrosopumilus maritimus.

Comments: Isolated from the marine archaeon Nitrosopumilus maritimus.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Metcalf, W.W., Griffin, B.M., Cicchillo, R.M., Gao, J., Janga, S.C., Cooke, H.A., Circello, B.T., Evans, B.S., Martens-Habbena, W., Stahl, D.A. and van der Donk, W.A. Synthesis of methylphosphonic acid by marine microbes: a source for methane in the aerobic ocean. Science 337 (2012) 1104-1107. [PMID: 22936780]

[EC 1.13.11.73 created 2012]

EC 1.13.11.74

Accepted name: 2-aminophenol 1,6-dioxygenase

Reaction: 2-aminophenol + O2 = 2-aminomuconate 6-semialdehyde

Other name(s): amnA (gene name); amnB (gene name); 2-aminophenol:oxygen 1,6-oxidoreductase (decyclizing)

Systematic name: 2-aminophenol:oxygen 1,6-oxidoreductase (ring-opening)

Comments: The enzyme, a member of the nonheme-iron(II)-dependent dioxygenase family, is an extradiol-type dioxygenase that utilizes a non-heme ferrous iron to cleave the aromatic ring at the meta position (relative to the hydroxyl substituent). The enzyme also has some activity with 2-amino-5-methylphenol and 2-amino-4-methylphenol [1]. The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.3.1.105, 2-amino-5-chlorophenol 1,6-dioxygenase [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Takenaka, S., Murakami, S., Shinke, R., Hatakeyama, K., Yukawa, H. and Aoki, K. Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme. J. Biol. Chem. 272 (1997) 14727-14732. [PMID: 9169437]

2. Wu, J.F., Sun, C.W., Jiang, C.Y., Liu, Z.P. and Liu, S.J. A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-chloronitrobenzene by Comamonas strain CNB-1: purification, properties, genetic cloning and expression in Escherichia coli. Arch. Microbiol. 183 (2005) 1-8. [PMID: 15580337]

3. Li, D.F., Zhang, J.Y., Hou, Y., Liu, L., Liu, S.J. and Liu, W. Crystallization and preliminary crystallographic analysis of 2-aminophenol 1,6-dioxygenase complexed with substrate and with an inhibitor. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68 (2012) 1337-1340. [PMID: 23143244]

[EC 1.13.11.74 created 2013]

EC 1.13.11.75

Accepted name: all-trans-8'-apo-β-carotenal 15,15'-oxygenase

Reaction: all-trans-8'-apo-β-carotenal + O2 = all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial

For diagram of reaction click here.

Other name(s): Diox1; ACO; 8'-apo-β-carotenal 15,15'-oxygenase

Systematic name: all-trans-8'-apo-β-carotenal:oxygen 15,15'-oxidoreductase (bond-cleaving)

Comments: Contains an Fe2+-4His arrangement. The enzyme is involved in retinal biosynthesis in bacteria [2].

Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:

References:

1. Ruch, S., Beyer, P., Ernst, H. and Al-Babili, S. Retinal biosynthesis in Eubacteria: in vitro characterization of a novel carotenoid oxygenase from Synechocystis sp. PCC 6803. Mol. Microbiol. 55 (2005) 1015-1024. [PMID: 15686550]

2. Kloer, D.P., Ruch, S., Al-Babili, S., Beyer, P. and Schulz, G.E. The structure of a retinal-forming carotenoid oxygenase. Science 308 (2005) 267-269. [PMID: 15821095]

[EC 1.13.11.75 created 2010 as EC 1.14.99.41, transferred 2013 to EC 1.13.11.75]

EC 1.13.11.76

Accepted name: 2-amino-5-chlorophenol 1,6-dioxygenase

Reaction: 2-amino-5-chlorophenol + O2 = 2-amino-5-chloromuconate 6-semialdehyde

Other name(s): cnbC (gene name); 2-amino-5-chlorophenol:oxygen 1,6-oxidoreductase (decyclizing)

Systematic name: 2-amino-5-chlorophenol:oxygen 1,6-oxidoreductase (ring-opening)

Comments: The enzyme, a member of the nonheme-iron(II)-dependent dioxygenase family, is an extradiol-type dioxygenase that utilizes a non-heme ferrous iron to cleave the aromatic ring at the meta position (relative to the hydroxyl substituent). The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.3.11.74, 2-aminophenol 1,6-dioxygenase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wu, J.F., Sun, C.W., Jiang, C.Y., Liu, Z.P. and Liu, S.J. A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-chloronitrobenzene by Comamonas strain CNB-1: purification, properties, genetic cloning and expression in Escherichia coli. Arch. Microbiol. 183 (2005) 1-8. [PMID: 15580337]

[EC 1.13.11.76 created 2013]

EC 1.13.11.77

Accepted name: oleate 10S-lipoxygenase

Reaction: (1) oleate + O2 = (8E,10S)-10-hydroperoxyoctadeca-8-enoate
(2) linoleate + O2 = (8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
(3) α-linolenate + O2 = (8E,10S,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate

Other name(s): 10S-DOX; (10S)-dioxygenase; 10S-dioxygenase

Systematic name: oleate:oxygen (10S)-oxidoreductase

Comments: Binds Fe2+. The enzyme isolated from the bacterium Pseudomonas sp. 42A2 has similar activity with all the three Δ9 fatty acids. cf. EC 1.13.11.62, linoleate 10R-lipoxygenase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Busquets, M., Deroncele, V., Vidal-Mas, J., Rodriguez, E., Guerrero, A. and Manresa, A. Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid. Antonie Van Leeuwenhoek 85 (2004) 129-139. [PMID: 15028873]

[EC 1.13.11.77 created 2013]

EC 1.13.11.78

Accepted name: 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming)

Reaction: (2-amino-1-hydroxyethyl)phosphonate + O2 = glycine + phosphate

Other name(s): phnZ (gene name)

Systematic name: 2-amino-1-hydroxyethylphosphonate:oxygen 1-oxidoreductase (glycine-forming)

Comments: Requires Fe2+. The enzyme, characterized from a marine bacterium, is involved in a 2-aminoethylphosphonate degradation pathway.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. McSorley, F.R., Wyatt, P.B., Martinez, A., DeLong, E.F., Hove-Jensen, B. and Zechel, D.L. PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon-phosphorus bond. J. Am. Chem. Soc. 134 (2012) 8364-8367. [PMID: 22564006]

2. Worsdorfer, B., Lingaraju, M., Yennawar, N.H., Boal, A.K., Krebs, C., Bollinger, J.M., Jr. and Pandelia, M.E. Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases. Proc. Natl. Acad. Sci. USA 110 (2013) 18874-18879. [PMID: 24198335]

[EC 1.13.11.78 created 2014]

EC 1.13.11.79

Accepted name: 5,6-dimethylbenzimidazole synthase

Reaction: FMNH2 + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + other product(s)

For diagram of reaction click here.

Other name(s): BluB

Systematic name: FMNH2 oxidoreductase (5,6-dimethylbenzimidazole-forming)

Comments: The enzyme catalyses a complex oxygen-dependent conversion of reduced flavin mononucleotide to form 5,6-dimethylbenzimidazole, the lower ligand of vitamin B12. This conversion involves many sequential steps in two distinct stages, and an alloxan intermediate that acts as a proton donor, a proton acceptor, and a hydride acceptor [4]. The C-2 of 5,6-dimethylbenzimidazole is derived from C-1' of the ribityl group of FMNH2 and 2-H from the ribityl 1'-pro-S-hydrogen. While D-erythrose 4-phosphate has been shown to be one of the byproducts, the nature of the other product(s) has not been verified yet.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Gray, M.J. and Escalante-Semerena, J.C. Single-enzyme conversion of FMNH2 to 5,6-dimethylbenzimidazole, the lower ligand of B12. Proc. Natl. Acad. Sci. USA 104 (2007) 2921-2926. [PMID: 17301238]

2. Ealick, S.E. and Begley, T.P. Biochemistry: molecular cannibalism. Nature 446 (2007) 387-388. [PMID: 17377573]

3. Taga, M.E., Larsen, N.A., Howard-Jones, A.R., Walsh, C.T. and Walker, G.C. BluB cannibalizes flavin to form the lower ligand of vitamin B12. Nature 446 (2007) 449. [PMID: 17377583]

4. Wang, X.L. and Quan, J.M. Intermediate-assisted multifunctional catalysis in the conversion of flavin to 5,6-dimethylbenzimidazole by BluB: a density functional theory study. J. Am. Chem. Soc. 133 (2011) 4079-4091. [PMID: 21344938]

[EC 1.13.11.79 created 2010 as EC 1.14.99.40, transferred 2014 to EC 1.13.11.79]

EC 1.13.11.80

Accepted name: (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase

Reaction: (3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA

Glossary: (3,5-dihydroxyphenyl)acetyl-CoA = 2-(3,5-dihydroxyphenyl)acetyl-CoA

Other name(s): DpgC

Systematic name: (3,5-dihydroxyphenyl)acetyl-CoA:oxygen oxidoreductase

Comments: The enzyme, characterized from bacteria Streptomyces toyocaensis and Amycolatopsis orientalis, is involved in the biosynthesis of (3,5-dihydroxyphenyl)glycine, a component of the glycopeptide antibiotic vancomycin.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Chen, H., Tseng, C.C., Hubbard, B.K. and Walsh, C.T. Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine. Proc. Natl. Acad. Sci. USA 98 (2001) 14901-14906. [PMID: 11752437]

2. Widboom, P.F., Fielding, E.N., Liu, Y. and Bruner, S.D. Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis. Nature 447 (2007) 342-345. [PMID: 17507985]

3. Fielding, E.N., Widboom, P.F. and Bruner, S.D. Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC. Biochemistry 46 (2007) 13994-14000. [PMID: 18004875]

[EC 1.13.11.80 created 2015]

EC 1.13.11.81

Accepted name: 7,8-dihydroneopterin oxygenase

Reaction: 7,8-dihydroneopterin + O2 = 7,8-dihydroxanthopterin + formate + glycolaldehyde

For diagram of reaction click here.

Glossary: 7,8-dihydroneopterin = 2-amino-6-[(1S,2R)-1,2,3-trihydroxypropyl]-7,8-dihydropteridin-4(3H)-one
7,8-dihydroxanthopterin = 2-amino-3,5,7,8-tetrahydropteridin-4,6-dione

Systematic name: 7,8-dihydroneopterin:oxygen oxidoreductase

Comments: The enzyme from the bacterium Mycobacterium tuberculosis is multifunctional and also catalyses the epimerisation of the 2'-hydroxy group of 7,8-dihydroneopterin (EC 5.1.99.8, 7,8-dihydroneopterin epimerase) and the reaction of EC 4.1.2.25 (dihydroneopterin aldolase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Czekster, C.M. and Blanchard, J.S. One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis. J. Am. Chem. Soc. 134 (2012) 19758-19771. [PMID: 23150985]

[EC 1.13.11.81 created 2015]

EC 1.13.11.82

Accepted name: 8'-apo-carotenoid 13,14-cleaving dioxygenase

Reaction: 8'-apo-β-carotenal + O2 = 13-apo-β-carotenone + 2,6-dimethyldeca-2,4,6,8-tetraenedial

For diagram of reaction click here.

Other name(s): NACOX1 (gene name)

Systematic name: 8'-apo-β-carotenal:oxygen 13,14-dioxygenase (bond-cleaving)

Comments: Isolated from the bacterium Novosphingobium aromaticivorans. It is less active with 4'-apo-β-carotenal and γ-carotene.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kim, Y.S., Seo, E.S. and Oh, D.K. Characterization of an apo-carotenoid 13,14-dioxygenase from Novosphingobium aromaticivorans that converts β-apo-8'-carotenal to β-apo-13-carotenone. Biotechnol. Lett. 34 (2012) 1851-1856. [PMID: 22711425]

[EC 1.13.11.82 created 2015]


Continued with EC 1.13.12 to EC 1.14.11
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