Enzyme Nomenclature

Continued from EC 1.14.13.1 to EC 1.14.13.50

EC 1.14.13 (Continued)

See separate file for EC 1.14.13.1 to EC 1.14.13.50
EC 1.14.13.101 to EC 1.14.13.150
EC 1.14.13.151 to EC 1.14.13.242

Contents

EC 1.14.13.51 6-oxocineole dehydrogenase
EC 1.14.13.52 isoflavone 3'-hydroxylase
EC 1.14.13.53 4'-methoxyisoflavone 2'-hydroxylase
EC 1.14.13.54 ketosteroid monooxygenase
EC 1.14.13.55 protopine 6-monooxygenase
EC 1.14.13.56 dihydrosanguinarine 10-monooxygenase
EC 1.14.13.57 dihydrochelirubine 12-monooxygenase
EC 1.14.13.58 benzoyl-CoA 3-monooxygenase
EC 1.14.13.59 L-lysine 6-monooxygenase (NADPH)
EC 1.14.13.60 27-hydroxycholesterol 7α-monooxygenase
EC 1.14.13.60 transferred now EC 1.14.13.100
EC 1.14.13.61 2-hydroxyquinoline 8-monooxygenase
EC 1.14.13.62 4-hydroxyquinoline 3-monooxygenase
EC 1.14.13.63 3-hydroxyphenylacetate 6-hydroxylase
EC 1.14.13.64 4-hydroxybenzoate 1-hydroxylase
EC 1.14.13.65 deleted
EC 1.14.13.66 2-hydroxycyclohexanone 2-monooxygenase
EC 1.14.13.67 transferred now EC 1.14.14.55
EC 1.14.13.68 transferred now EC 1.14.14.37
EC 1.14.13.69 alkene monooxygenase
EC 1.14.13.70 sterol 14α-demethylase
EC 1.14.13.71 N-methylcoclaurine 3'-monooxygenase
EC 1.14.13.72 transferred now EC 1.14.18.9
EC 1.14.13.73 tabersonine 16-hydroxylase
EC 1.14.13.74 transferred now EC 1.14.14.85
EC 1.14.13.75 vinorine hydroxylase
EC 1.14.13.76 taxane 10β-hydroxylase
EC 1.14.13.77 taxane 13α-hydroxylase
EC 1.14.13.78 transferred now EC 1.14.14.86
EC 1.14.13.79 ent-kaurenoic acid oxidase
EC 1.14.13.80 transferred now EC 1.14.14.53
EC 1.14.13.81 magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase
EC 1.14.13.82 vanillate monooxygenase
EC 1.14.13.83 precorrin-3B synthase
EC 1.14.13.84 4-hydroxyacetophenone monooxygenase
EC 1.14.13.85 glyceollin synthase
EC 1.14.13.86 deleted
EC 1.14.13.87 licodione synthase
EC 1.14.13.88 transferred now EC 1.14.14.81
EC 1.14.13.89 isoflavone 2'-hydroxylase
EC 1.14.13.90 transferred now EC 1.14.15.21
EC 1.14.13.91 deoxysarpagine hydroxylase
EC 1.14.13.92 phenylacetone monooxygenase
EC 1.14.13.93 (+)-abscisic acid 8'-hydroxylase
EC 1.14.13.94 lithocholate 6β-hydroxylase
EC 1.14.13.95 transferred now EC 1.14.18.8
EC 1.14.13.96 5β-cholestane-3α,7α-diol 12α-hydroxylase
EC 1.14.13.97 transferred now EC 1.14.14.57
EC 1.14.13.98 transferred now EC 1.14.14.25
EC 1.14.13.99 transferred now EC 1.14.14.26
EC 1.14.13.100 transferred now EC 1.14.14.29

See the following files for:
EC 1.14.13.101 to EC 1.14.13.150
EC 1.14.13.151 to EC 1.14.13.242

EC 1.14.13.51

Accepted name: 6-oxocineole dehydrogenase

Reaction: 6-oxocineole + NADPH + H+ + O2 = 1,6,6-trimethyl-2,7-dioxabicyclo[3.2.2]nonan-3-one + NADP+ + H2O

For diagram of reaction click here.

Other name(s): 6-oxocineole oxygenase

Systematic name: 6-oxocineole,NADPH:oxygen oxidoreductase

Comments: The product undergoes non-enzymic cleavage and subsequent ring closure to form the lactone 4,5-dihydro-5,5-dimethyl-4-(3-oxobutyl)furan-2(3H)-one.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122933-80-6

References:

1. Williams, D.R., Trudgill, P.W. and Taylor, D.G. Metabolism of 1,8-cineole by a Rhodococcus species - ring cleavage reactions. J. Gen. Microbiol. 135 (1989) 1957-1967.

[EC 1.14.13.51 created 1992]

[EC 1.14.13.52 Transferred entry: isoflavone 3'-hydroxylase. Now EC 1.14.14.88, isoflavone 3'-hydroxylase (EC 1.14.13.52 created 1992, deleted 2018)]

[EC 1.14.13.53 Transferred entry: 4'-methoxyisoflavone 2'-hydroxylase. Now EC 1.14.14.89, 4'-methoxyisoflavone 2'-hydroxylase (EC 1.14.13.53 created 1992, modified 2005, deleted 2018)]

EC 1.14.13.54

Accepted name: ketosteroid monooxygenase

Reaction: a ketosteroid + NADPH + H+ + O2 = a steroid ester/lactone + NADP+ + H2O (general reaction)
(1) progesterone + NADPH + H+ + O2 = testosterone acetate + NADP+ + H2O
(2) androstenedione + NADPH + H+ + O2 = testololactone + NADP+ + H2O
(3) 17α-hydroxyprogesterone + NADPH + H+ + O2 = androstenedione + acetate + NADP+ + H2O

Glossary: progesterone = pregn-4-ene-3,20-dione
testosterone acetate = 3-oxoandrost-4-en-17β-yl acetate
androstenedione = androst-4-ene-3,17-dione
testololactone = 3-oxo-13,17-secoandrost-4-eno-17,13α-lactone
17α-hydroxyprogesterone = 17α-hydroxypregn-4-ene-3,20-dione

Other name(s): steroid-ketone monooxygenase; progesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, ester-producing); 17α-hydroxyprogesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, side-chain cleaving); androstenedione, NADPH2:oxygen oxidoreductase (17-hydroxylating, lactonizing)

Systematic name: ketosteroid,NADPH:oxygen oxidoreductase (20-hydroxylating, ester-producing/20-hydroxylating, side-chain cleaving/17-hydroxylating, lactonizing)

Comments: A single FAD-containing enzyme catalyses three types of monooxygenase (Baeyer-Villiger oxidation) reaction. The oxidative esterification of a number of derivatives of progesterone to produce the corresponding 17α-hydroxysteroid 17-acetate ester, such as testosterone acetate, is shown in Reaction (1). The oxidative lactonization of a number of derivatives of androstenedione to produce the 13,17-secoandrosteno-17,13α-lactone, such as testololactone, is shown in Reaction (2). The oxidative cleavage of the 17β-side-chain of 17α-hydroxyprogesterone to produce androstenedione and acetate is shown in Reaction (3). Reaction (1) is also catalysed by EC 1.14.99.4 (progesterone monooxygenase), and Reactions (2) and (3) correspond to that catalysed by EC 1.14.99.12 (androst-4-ene-3,17-dione monooxygenase). The possibility that a single enzyme is responsible for the reactions ascribed to EC 1.14.99.4 and EC 1.14.99.12 in other tissues cannot be excluded.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9044-53-5

References:

1. Katagiri, M. and Itagaki, E. A steroid ketone monooxygenase from Cylindrocarpon radicicola. in Chemistry and Biochemistry of Flavoenzymes, (Müller, F., ed.) (1991) pp. 102-108, CRC Press, Florida.

2. Itagaki, E. Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Purification and characterization. J. Biochem. (Tokyo) 99 (1986) 815-824. [PMID: 3486863]

3. Itagaki, E. Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC11011. Oxygenative lactonization of androstenedione to testololactone. J. Biochem. (Tokyo) 99 (1986) 825-832. [PMID: 3486864]

[EC 1.14.13.54 created 1999]

[EC 1.14.13.55 Transferred entry: protopine 6-monooxygenase. Now EC 1.14.14.98, protopine 6-monooxygenase (EC 1.14.13.55 created 1999, deleted 2018)]

[EC 1.14.13.56 Transferred entry: dihydrosanguinarine 10-monooxygenase. Now EC 1.14.14.100, dihydrosanguinarine 10-monooxygenase (EC 1.14.13.56 created 1999, deleted 2018)]

[EC 1.14.13.57 Transferred entry: dihydrochelirubine 12-monooxygenase. Now EC 1.14.14.101, dihydrochelirubine 12-monooxygenase (EC 1.14.13.57 created 1999, deleted 2018)]

EC 1.14.13.58

Accepted name: benzoyl-CoA 3-monooxygenase

Reaction: benzoyl-CoA + NADPH + H+ + O2 = 3-hydroxybenzoyl-CoA + NADP+ + H2O

Other name(s): benzoyl-CoA 3-hydroxylase

Systematic name: benzoyl-CoA,NADPH:oxygen oxidoreductase (3-hydroxylating)

Comments: the enzyme from the denitrifying bacterium Pseudomonas KB740 catalyses a flavin-requiring reaction (FAD or FMN). Benzoate is not a substrate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 151616-61-4

References:

1. Niemetz, R., Altenschmidt, U., Herrmann, H. and Fuchs, G. Benzoyl-coenzyme-A 3-monooxygenase, a flavin-dependent hydroxylase. Purification, some properties and its role in aerobic benzoate oxidation via gentisate in a denitrifying bacterium. Eur. J. Biochem. 227 (1995) 161-168. [PMID: 7851381]

[EC 1.14.13.58 created 1999]

EC 1.14.13.59

Accepted name: L-lysine N6-monooxygenase (NADPH)

Reaction: L-lysine + NADPH + H+ + O2 = N6-hydroxy-L-lysine + NADP+ + H2O

For diagram of reaction click here

Other name(s): lysine N6-hydroxylase; L-lysine 6-monooxygenase (NADPH) (ambiguous)

Systematic name: L-lysine,NADPH:oxygen oxidoreductase (6-hydroxylating)

Comments: A flavoprotein (FAD). The enzyme from strain EN 222 of Escherichia coli is highly specific for L-lysine; L-ornithine and L-homolysine are, for example, not substrates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 64295-82-5

References:

1. Plattner, H.J., Pfefferle, P., Romaguera, A., Waschutza, S. and Diekmann, H. Isolation and some properties of lysine N6-hydroxylase from Escherichia coli strain EN222. Biol. Met. 2 (1989) 1-5. [PMID: 2518519]

2. Macheroux, P., Plattner, H.J., Romaguera, A. and Diekmann, H. FAD and substrate analogs as probes for lysine N6-hydroxylase from Escherichia coli EN 222. Eur. J. Biochem. 213 (1993) 995-1002. [PMID: 8504838]

3. Thariath, A.M., Fatum, K.L., Valvano, M.A. and Viswanatha, T. Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase. Biochim. Biophys. Acta 1203 (1993) 27-35. [PMID: 8218389]

4. de Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570-578. [PMID: 2935523]

5. Marrone, L., Siemann, S., Beecroft, M. and Viswanatha, T. Specificity of lysine:N-6-hydroxylase: A hypothesis for a reactive substrate intermediate in the catalytic mechanism. Bioorg. Chem. 24 (1996) 401-406.

6. Goh, C.J., Szczepan, E.W., Menhart, N. and Viswanatha, T. Studies on lysine: N6-hydroxylation by cell-free system of Aerobacter aerogenes 62-1. Biochim. Biophys. Acta 990 (1989) 240-245. [PMID: 2493814]

[EC 1.14.13.59 created 1999, modified 2001, modified 2012]

[EC 1.14.13.60 Transferred entry: 27-hydroxycholesterol 7α-monooxygenase. Now included with EC 1.14.13.100, 25/26-hydroxycholesterol 7α-hydroxylase (EC 1.14.13.60 created 1999, deleted 2013)]

EC 1.14.13.60

Accepted name: 27-hydroxycholesterol 7α-monooxygenase

Reaction: 27-hydroxycholesterol + NADPH + H+ + O2 = 7α,27-dihydroxycholesterol + NADP+ + H2O

For diagram click here.

Other name(s): 27-hydroxycholesterol 7α-hydroxylase

Systematic name: 27-hydroxycholesterol,NADPH:oxygen oxidoreductase (7α-hydroxylating)

Comments: a heme-thiolate protein (P-450). The enzyme from mammalian liver differs from cholesterol 7α-monooxygenase (EC 1.14.13.17) in having no activity towards cholesterol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 149316-80-3

References:

1. Kumiko, O.M., Budai, K. and Javitt, N.B. Cholesterol and 27-hydroxycholesterol 7α-hydroxylation: evidence for two different enzymes. J. Lipid Res. 34 (1993) 581-588.

[EC 1.14.13.60 created 1999]

EC 1.14.13.61

Accepted name: 2-hydroxyquinoline 8-monooxygenase

Reaction: quinolin-2-ol + NADH + H+ + O2 = quinolin-2,8-diol + NAD+ + H2O

Other name(s): 2-oxo-1,2-dihydroquinoline 8-monooxygenase

Systematic name: quinolin-2(1H)-one, NADH:oxygen oxidoreductase (8-oxygenating)

Comments: requires iron. Quinolin-2-ol exists largely as the quinolin-2(1H)-one tautomer.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 166799-89-9

References:

1. Rosche, B., Tshisuaka, B., Fetzner, S. and Lingens, F. 2-Oxo-1,2-dihydroquinoline 8-monooxygenase, a two-component enzyme system from Pseudomonas putida 86. J. Biol. Chem. 270 (1995) 17836-17842. [PMID: 7629085]

[EC 1.14.13.61 created 1999]

EC 1.14.13.62

Accepted name: 4-hydroxyquinoline 3-monooxygenase

Reaction: quinolin-4-ol + NADH + H+ + O2 = quinolin-3,4-diol + NAD+ + H2O

Other name(s): quinolin-4(1H)-one 3-monooxygenase

Systematic name: quinolin-4(1H)-one,NADH:oxygen oxidoreductase (3-oxygenating)

Comments: quinolin-4-ol exists largely as the quinolin-4(1H)-one tautomer.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 144378-37-0

References:

1. Block, D.W. and Lingens, F. Microbial metabolism of quinoline and related compounds. XIV. Purification and properties of 1H-3-hydroxy-4-oxoquinoline oxygenase, a new estradiol cleavage enzyme from Pseudomonas putida strain 33/1. Biol. Chem. Hoppe Seyler 373 (1992) 249-254. [PMID: 1627263]

[EC 1.14.13.62 created 1999]

EC 1.14.13.63

Accepted name: 3-hydroxyphenylacetate 6-hydroxylase

Reaction: 3-hydroxyphenylacetate + NAD(P)H + H+ + O2 = 2,5-dihydroxyphenylacetate + NAD(P)+ + H2O

For diagram of reaction click here.

Glossary: homogentisate = 2,5-dihydroxyphenylacetate

Other name(s): 3-hydroxyphenylacetate 6-monooxygenase

Systematic name: 3-hydroxyphenylacetate,NAD(P)H:oxygen oxidoreductase (6-hydroxylating)

Comments: 3-hydroxyphenylacetate 6-hydroxylase from Flavobacterium sp. is highly specific for 3-hydroxyphenylacetate and uses NADH and NADPH as electron donors with similar efficiency.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 114705-01-0

References:

1. van Berkel, W.H.J. and van den Tweel, W.J.J. Purification and characterisation of 3-hydroxyphenylacetate 6-hydroxylase: a novel FAD-dependent monooxygenase from a Flavobacterium sp. Eur. J. Biochem. 201 (1991) 585-592. [PMID: 1935954]

[EC 1.14.13.63 created 1999]

EC 1.14.13.64

Accepted name: 4-hydroxybenzoate 1-hydroxylase

Reaction: 4-hydroxybenzoate + NAD(P)H + 2 H+ + O2 = hydroquinone + NAD(P)+ + H2O + CO2

Other name(s): 4-hydroxybenzoate 1-monooxygenase

Systematic name: 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating, decarboxylating)

Comments: requires FAD. The enzyme from Candida parapsilosis is specific for 4-hydroxybenzoate derivatives and prefers NADH to NADPH as electron donor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD , CAS registry number: 134214-78-1

References:

1. van Berkel, W.J.H., Eppink, M.H.M., Middelhoven, W.J., Vervoort, J. and Rietjens, I.M.C.M. Catabolism of 4-hydroxybenzoate in Candida parapsilosis proceeds through initial oxidative decarboxylation by a FAD-dependent 4-hydroxybenzoate 1-hydroxylase. FEMS Microbiol. Lett. 121 (1994) 207-216. [PMID: 7926672]

[EC 1.14.13.64 created 1999]

[EC 1.14.13.65 Deleted entry: 2-hydroxyquinoline 8-monooxygenase (EC 1.14.13.65 created 1999, deleted 2006)]

EC 1.14.13.66

Accepted name: 2-hydroxycyclohexanone 2-monooxygenase

Reaction: 2-hydroxycyclohexan-1-one + NADPH + H+ + O2 = 6-hydroxyhexan-6-olide + NADP+ + H2O

Systematic name: 2-hydroxycyclohexan-1-one,NADPH:oxygen 2-oxidoreductase (1,2-lactonizing)

Comment: the product decomposes spontaneously to 6-oxohexanoic acid (adipic semialdehyde).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62628-31-3

References

1. Davey, J.F. and Trudgill, P.W. The metabolism of trans-cyclohexan-1,2-diol by an Acinetobacter species. Eur. J. Biochem. 74 (1977) 115-127. [PMID: 856571]

[EC 1.14.13.66 created 1978 as EC 1.14.12.6, transferred 1999 to EC 1.14.13.66]

[EC 1.14.13.67 Transferred entry: quinine 3-monooxygenase. Now EC 1.14.14.55, quinine 3-monooxygenase (EC 1.14.13.67 created 2000, deleted 2017)]

[EC 1.14.13.68 Transferred entry: 4-hydroxyphenylacetaldehyde oxime monooxygenase, now EC 1.14.14.37, 4-hydroxyphenylacetaldehyde oxime monooxygenase (EC 1.14.13.68 created 2000, modified 2005, deleted 2016)]

EC 1.14.13.69

Accepted name: alkene monooxygenase

Reaction: propene + NADH + H+ + O2 = 1,2-epoxypropane + NAD+ + H2O

For diagram click here.

Other name(s): alkene epoxygenase

Systematic name: alkene,NADH:oxygen oxidoreductase

Comments: This bacterial binuclear non-heme iron enzyme is a multicomponent enzyme complex comprising an oxygenase, a reductase, and a Rieske-type ferredoxin. The enzyme from the bacterium Xanthobacter sp. strain Py2 contains an additional small protein of unknown function that is essential for activity. In general, the enzyme oxygenates C2 to C6 aliphatic alkenes, although enzymes from different organisms show different substrate range. With propene as substrate, the stereospecificity of the epoxypropane formed is 95% (R) and 5% (S).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 63439-50-9

References:

1. Small, F.J. and Ensign, S.A. Alkene monooxygenase from Xanthobacter strain Py2: purification and characterization of a four-component system central to the bacterial metabolism of aliphatic alkenes. J. Biol. Chem. 272 (1997) 24913-24920. [PMID: 9312093]

2. Zhou, N.Y., Jenkins, A., Chion, C.K.N.C.K. and Leak, D.J. The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol. Appl. Environ. Microbiol. 65 (1999) 1589-1595. [PMID: 10103255]

3. Gallagher, S.C., Cammack, R. and Dalton, H. Alkene monooxygenase from Nocardia corallina B-276 is a member of the class of dinuclear iron proteins capable of stereospecific epoxygenation reactions. Eur. J. Biochem. 247 (1997) 635-641. [PMID: 9266707]

[EC 1.14.13.69 created 2001]

[EC 1.14.13.70 Transferred entry: sterol 14α-demethylase. Now EC 1.14.14.154, sterol 14α-demethylase (EC 1.14.13.70 created 2001, modified 2013, deleted 2018)]

[EC 1.14.13.71 Transferred entry: N-methylcoclaurine 3'-monooxygenase. Now EC 1.14.14.102, N-methylcoclaurine 3'-monooxygenase (EC 1.14.13.71 created 2001, deleted 2018)]

[EC 1.14.13.72 Transferred entry: methylsterol monooxygenase. Now classified as EC 1.14.18.9, methylsterol monooxygenase (EC 1.14.13.72 created 1972 as EC 1.14.99.16, transferred 2002 to EC 1.14.13.72, deleted 2017)]

[EC 1.14.13.73 Transferred entry: tabersonine 16-hydroxylase. Now EC 1.14.14.103, tabersonine 16-hydroxylase (EC 1.14.13.73 created 2002, deleted 2018)]

[EC 1.14.13.74 Transferred entry: 7-deoxyloganin 7-hydroxylase. Now EC 1.14.14.85, 7-deoxyloganin 7-hydroxylase (EC 1.14.13.74 created 2002, deleted 2018)]

[EC 1.14.13.75 Transferred entry: vinorine hydroxylase. Now EC 1.14.14.104, vinorine hydroxylase (EC 1.14.13.75 created 2002, deleted 2018)]

[EC 1.14.13.76 Transferred entry: taxane 10β-hydroxylase. Now EC 1.14.14.105, taxane 10β-hydroxylase (EC 1.14.13.76 created 2002, deleted 2018)]

[EC 1.14.13.77 Transferred entry: taxane 13α-hydroxylase. Now EC 1.14.14.106, taxane 13α-hydroxylase (EC 1.14.13.77 created 2002, deleted 2018)]

[EC 1.14.13.78 Transferred entry: ent-kaurene oxidase. Now EC 1.14.14.86, ent-kaurene monooxygenase (EC 1.14.13.78 created 2002, deleted 2018)]

[EC 1.14.13.79 Transferred entry: ent-kaurenoic acid oxidase. Now EC 1.14.14.107, ent-kaurenoic acid oxidase (EC 1.14.13.79 created 2002, deleted 2018)]

[EC 1.14.13.80 Transferred entry: (R)-limonene 6-monooxygenase. Now classified as EC 1.14.14.53, (R)-limonene 6-monooxygenase (EC 1.14.13.80 created 2003, deleted 2017)]

EC 1.14.13.81

Accepted name: magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase

Reaction: magnesium-protoporphyrin IX 13-monomethyl ester + 3 NADPH + 3 H+ + 3 O2 = 3,8-divinyl protochlorophyllide a + 3 NADP+ + 5 H2O (overall reaction)
(1a) magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + H+ + O2 = 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + NADP+ + H2O
(1b) 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + H+ + O2 = 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + NADP+ + 2 H2O
(1c) 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + H+ + O2 = 3,8-divinyl protochlorophyllide a + NADP+ + 2 H2O

For diagram of reaction click here.

Other name(s): Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase

Systematic name: magnesium-protoporphyrin-IX 13-monomethyl ester,NADPH:oxygen oxidoreductase (hydroxylating)

Comments: Requires Fe(II) for activity. The enzyme participates in the biosynthesis of chlorophyllide a in aerobic organisms. The same transformation is achieved in anaerobic organisms by EC 1.21.98.3, anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase. Some facultative phototrophic bacteria, such as Rubrivivax gelatinosus, possess both enzymes.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 92353-62-3

References:

1. Walker, C.J., Mansfield, K.E., Rezzano, I.N., Hanamoto, C.M., Smith, K.M. and Castelfranco, P.A. The magnesium-protoporphyrin IX (oxidative) cyclase system. Studies on the mechanism and specificity of the reaction sequence. Biochem. J. 255 (1988) 685-692. [PMID: 3202840]

2. Bollivar, D.W. and Beale, S.I. The chlorophyll biosynthetic enzyme Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase (characterization and partial purification from Chlamydomonas reinhardtii and Synechocystis sp. PCC 6803). Plant Physiol. 112 (1996) 105-114. [PMID: 12226378]

3. Pinta, V., Picaud, M., Reiss-Husson, F. and Astier, C. Rubrivivax gelatinosus acsF (previously orf358) codes for a conserved, putative binuclear-iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethylester. J. Bacteriol. 184 (2002) 746-753. [PMID: 11790744]

4. Tottey, S., Block, M.A., Allen, M., Westergren, T., Albrieux, C., Scheller, H.V., Merchant, S. and Jensen, P.E. Arabidopsis CHL27, located in both envelope and thylakoid membranes, is required for the synthesis of protochlorophyllide. Proc. Natl. Acad. Sci. USA 100 (2003) 16119-16124. [PMID: 14673103]

[EC 1.14.13.81 created 2003, modified 2017]

EC 1.14.13.82

Accepted name: vanillate monooxygenase

Reaction: vanillate + O2 + NADH + H+ = 3,4-dihydroxybenzoate + NAD+ + H2O + formaldehyde

For diagram of reaction click here

Glossary entries: vanillate = 4-hydroxy-3-methoxybenzoate

Other name(s): 4-hydroxy-3-methoxybenzoate demethylase; vanillate demethylase

Systematic name: vanillate:oxygen oxidoreductase (demethylating)

Comments: Forms part of the vanillin degradation pathway in Arthrobacter sp.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 39307-11-4

References:

1. Brunel, F. and Davison, J. Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase. J. Bacteriol. 170 (1988) 4924-4930. [PMID: 3170489]

2. Priefert, H., Rabenhorst, J. and Steinbuchel, A. Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate. J. Bacteriol. 179 (1997) 2595-2607. [PMID: 9098058]

[EC 1.14.13.82 created 2000 as EC 1.2.3.12, transferred 2003 to EC 1.14.13.82]

EC 1.14.13.83

Accepted name: precorrin-3B synthase

Reaction: precorrin-3A + NADH + H+ + O2 = precorrin-3B + NAD+ + H2O

For diagram click here and mechanism here.

Other name(s): precorrin-3X synthase; CobG

Systematic name: precorrin-3A,NADH:oxygen oxidoreductase (20-hydroxylating)

Comments: An iron-sulfur protein. An oxygen atom from dioxygen is incorporated into the macrocycle at C-20. In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. The first of the four steps is carried out by EC 1.14.13.83, precorrin-3B synthase (CobG), yielding precorrin-3B as the product. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 152787-63-8

References:

1. Debussche, L., Thibaut, D., Cameron, B., Crouzet, J. and Blanche, F. Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas denitrificans. J. Bacteriol. 175 (1993) 7430-7440. [PMID: 8226690]

2. Scott, A.I., Roessner, C.A., Stolowich, N.J., Spencer, J.B., Min, C. and Ozaki, S.I. Biosynthesis of vitamin B12. Discovery of the enzymes for oxidative ring contraction and insertion of the fourth methyl group. FEBS Lett. 331 (1993) 105-108. [PMID: 8405386]

3. Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C. The biosynthesis of adenosylcobalamin (vitamin B12). Nat. Prod. Rep. 19 (2002) 390-412. [PMID: 12195810]

[EC 1.14.13.83 created 2004]

EC 1.14.13.84

Accepted name: 4-hydroxyacetophenone monooxygenase

Reaction: (4-hydroxyphenyl)ethan-1-one + NADPH + H+ + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O

For diagram of reaction click here.

Other name(s): HAPMO

Systematic name: (4-hydroxyphenyl)ethan-1-one,NADPH:oxygen oxidoreductase (ester-forming)

Comments: Contains FAD. The enzyme from Pseudomonas fluorescens ACB catalyses the conversion of a wide range of acetophenone derivatives. Highest activity occurs with compounds bearing an electron-donating substituent at the para position of the aromatic ring [1]. In the absence of substrate, the enzyme can act as an NAD(P)H oxidase (EC 1.6.3.1).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 156621-13-5

References:

1. Kamerbeek, N.M., Moonen, M.J., van der Ven, J.G., van Berkel, W.J.H., Fraaije, M.W. and Janssen, D.B. 4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB: a novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds. Eur. J. Biochem. 268 (2001) 2547-2557. [PMID: 11322873 ]

2. Kamerbeek, N.M, Olsthoorn, A.J.J., Fraaije, M.W. and Janssen, D.B. Substrate specificity of a novel Baeyer-Villiger monooxygenase, 4-hydroxyacetophenone monooxygenase. Appl. Environ. Microbiol. 69 (2003) 419-426. [PMID: 12514023]

[EC 1.14.13.84 created 2004]

[EC 1.14.13.85 Transferred entry: glyceollin synthase. Now EC 1.14.14.135, glyceollin synthase (EC 1.14.13.85 created 2004, deleted 2018)]

[EC 1.14.13.86 Deleted entry: 2-hydroxyisoflavanone synthase. This enzyme was classified on the basis of an incorrect reaction. The activity is covered by EC 1.14.14.87 2-hydroxyisoflavanone synthase (EC 1.14.13.86 created 2004, deleted 2013)]

[EC 1.14.13.87 Transferred entry: licodione synthase. Now EC 1.14.14.140, licodione synthase (EC 1.14.13.87 created 2004, deleted 2018)]

[EC 1.14.13.88 Transferred entry: flavanoid 3',5'-hydroxylase. Now EC 1.14.14.81, flavanoid 3',5'-hydroxylase (EC 1.14.13.88 created 2004, deleted 2018)]

[EC 1.14.13.89 Transferred entry: isoflavone 2-hydroxylase. Now EC 1.14.14.90, isoflavone 2-hydroxylase (EC 1.14.13.89 created 2005, deleted 2018)]

[EC 1.14.13.90 Transferred entry: zeaxanthin epoxidase. Now EC 1.14.15.21, zeaxanthin epoxidase (EC 1.14.13.90 created 2005, deleted 2016)]

[EC 1.14.13.91 Transferred entry: deoxysarpagine hydroxylase. Now EC 1.14.14.136, deoxysarpagine hydroxylase (EC 1.14.13.91 created 2005, deleted 2018)]

EC 1.14.13.92

Accepted name: phenylacetone monooxygenase

Reaction: phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O

For diagram click here.

Other name(s): PAMO

Systematic name: phenylacetone,NADPH:oxygen oxidoreductase

Comments: A flavoprotein (FAD). NADH cannot replace NADPH as coenzyme. In addition to phenylacetone, which is the best substrate found to date, this Baeyer-Villiger monooxygenase can oxidize other aromatic ketones [1-(4-hydroxyphenyl)propan-2-one, 1-(4-hydroxyphenyl)propan-2-one and 3-phenylbutan-2-one], some alipatic ketones (e.g. dodecan-2-one) and sulfides (e.g. 1-methyl-4-(methylsulfanyl)benzene).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 1005768-90-0

References:

1. Malito, E., Alfieri, A., Fraaije, M.W. and Mattevi, A. Crystal structure of a Baeyer-Villiger monooxygenase. Proc. Natl. Acad. Sci. USA 101 (2004) 13157-13162. [PMID: 15328411]

2. Fraaije, M.W., Wu, J., Heuts, D.P., van Hellemond, E.W., Spelberg, J.H. and Janssen, D.B. Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining. Appl. Microbiol. Biotechnol. 66 (2005) 393-400. [PMID: 15599520]

[EC 1.14.13.92 created 2005]

[EC 1.14.13.93 Transferred entry: (+)-abscisic acid 8-hydroxylase. Now EC 1.14.14.137, (+)-abscisic acid 8-hydroxylase (EC 1.14.13.93 created 2005, deleted 2018)]

[EC 1.14.13.94 Transferred entry: lithocholate 6β-hydroxylase. Now EC 1.14.14.138, lithocholate 6β-hydroxylase (EC 1.14.13.94 created 2005, deleted 2018)]

[EC 1.14.13.95 Transferred entry: 7α-hydroxycholest-4-en-3-one 12α-hydroxylase. Now EC 1.14.18.8, 7α-hydroxycholest-4-en-3-one 12α-hydroxylase (EC 1.14.13.95 created 2005, deleted 2015)]

[EC 1.14.13.96 Transferred entry: 5β-cholestane-3α,7α-diol 12α-hydroxylase. Now EC 1.14.14.139, 5β-cholestane-3α,7α-diol 12α-hydroxylase (EC 1.14.13.96 created 2005, deleted 2018)]

[EC 1.14.13.97 Transferred entry: taurochenodeoxycholate 6α-hydroxylase. Now EC 1.14.14.57, taurochenodeoxycholate 6α-hydroxylase (EC 1.14.13.97 created 2005, deleted 2018)]

[EC 1.14.13.98 Transferred entry: cholesterol 24-hydroxylase, Now EC 1.14.14.25, cholesterol 24-hydroxylase (EC 1.14.13.98 created 2005, deleted 2016)]

[EC 1.14.13.99 Transferred entry: 24-hydroxycholesterol 7α-hydroxylase, now classified as EC 1.14.14.26, 24-hydroxycholesterol 7α-hydroxylase (EC 1.14.13.99 created 2005, deleted 2016)]

[EC 1.14.13.100 Transferred entry: 25/26-hydroxycholesterol 7α-hydroxylase. Now classified as EC 1.14.14.29, 25/26-hydroxycholesterol 7α-hydroxylase (EC 1.14.13.100 created 2005, modified 2013 (EC 1.14.13.60 created 1999, incorporated 2013), deleted 2016)]


Continued with EC 1.14.13.101 to EC 1.14.13.150
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