Continued from EC 126.96.36.199 to EC 188.8.131.52
EC 184.108.40.206 to EC 220.127.116.11
EC 18.104.22.168 to EC 22.214.171.124
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
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 126.96.36.199 Transferred entry: isoflavone 3'-hydroxylase. Now EC 188.8.131.52, isoflavone 3'-hydroxylase (EC 184.108.40.206 created 1992, deleted 2018)]
[EC 220.127.116.11 Transferred entry: 4'-methoxyisoflavone 2'-hydroxylase. Now EC 18.104.22.168, 4'-methoxyisoflavone 2'-hydroxylase (EC 22.214.171.124 created 1992, modified 2005, deleted 2018)]
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 126.96.36.199 (progesterone monooxygenase), and Reactions (2) and (3) correspond to that catalysed by EC 188.8.131.52 (androst-4-ene-3,17-dione monooxygenase). The possibility that a single enzyme is responsible for the reactions ascribed to EC 184.108.40.206 and EC 220.127.116.11 in other tissues cannot be excluded.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9044-53-5
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 18.104.22.168 Transferred entry: protopine 6-monooxygenase. Now EC 22.214.171.124, protopine 6-monooxygenase (EC 126.96.36.199 created 1999, deleted 2018)]
[EC 188.8.131.52 Transferred entry: dihydrosanguinarine 10-monooxygenase. Now EC 184.108.40.206, dihydrosanguinarine 10-monooxygenase (EC 220.127.116.11 created 1999, deleted 2018)]
[EC 18.104.22.168 Transferred entry: dihydrochelirubine 12-monooxygenase. Now EC 22.214.171.124, dihydrochelirubine 12-monooxygenase (EC 126.96.36.199 created 1999, deleted 2018)]
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
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]
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
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 188.8.131.52 Transferred entry: 27-hydroxycholesterol 7α-monooxygenase. Now included with EC 184.108.40.206, 25/26-hydroxycholesterol 7α-hydroxylase (EC 220.127.116.11 created 1999, deleted 2013)]
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 18.104.22.168) in having no activity towards cholesterol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 149316-80-3
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.
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
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]
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
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]
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
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]
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
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 22.214.171.124 Deleted entry: 2-hydroxyquinoline 8-monooxygenase (EC 126.96.36.199 created 1999, deleted 2006)]
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
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 188.8.131.52 Transferred entry: quinine 3-monooxygenase. Now EC 184.108.40.206, quinine 3-monooxygenase (EC 220.127.116.11 created 2000, deleted 2017)]
[EC 18.104.22.168 Transferred entry: 4-hydroxyphenylacetaldehyde oxime monooxygenase, now EC 22.214.171.124, 4-hydroxyphenylacetaldehyde oxime monooxygenase (EC 126.96.36.199 created 2000, modified 2005, deleted 2016)]
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
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 188.8.131.52 Transferred entry: sterol 14α-demethylase. Now EC 184.108.40.206, sterol 14α-demethylase (EC 220.127.116.11 created 2001, modified 2013, deleted 2018)]
[EC 18.104.22.168 Transferred entry: N-methylcoclaurine 3'-monooxygenase. Now EC 22.214.171.124, N-methylcoclaurine 3'-monooxygenase (EC 126.96.36.199 created 2001, deleted 2018)]
[EC 188.8.131.52 Transferred entry: methylsterol monooxygenase. Now classified as EC 184.108.40.206, methylsterol monooxygenase (EC 220.127.116.11 created 1972 as EC 18.104.22.168, transferred 2002 to EC 22.214.171.124, deleted 2017)]
[EC 126.96.36.199 Transferred entry: tabersonine 16-hydroxylase. Now EC 188.8.131.52, tabersonine 16-hydroxylase (EC 184.108.40.206 created 2002, deleted 2018)]
[EC 220.127.116.11 Transferred entry: 7-deoxyloganin 7-hydroxylase. Now EC 18.104.22.168, 7-deoxyloganin 7-hydroxylase (EC 22.214.171.124 created 2002, deleted 2018)]
[EC 126.96.36.199 Transferred entry: vinorine hydroxylase. Now EC 188.8.131.52, vinorine hydroxylase (EC 184.108.40.206 created 2002, deleted 2018)]
[EC 220.127.116.11 Transferred entry: taxane 10β-hydroxylase. Now EC 18.104.22.168, taxane 10β-hydroxylase (EC 22.214.171.124 created 2002, deleted 2018)]
[EC 126.96.36.199 Transferred entry: taxane 13α-hydroxylase. Now EC 188.8.131.52, taxane 13α-hydroxylase (EC 184.108.40.206 created 2002, deleted 2018)]
[EC 220.127.116.11 Transferred entry: ent-kaurene oxidase. Now EC 18.104.22.168, ent-kaurene monooxygenase (EC 22.214.171.124 created 2002, deleted 2018)]
[EC 126.96.36.199 Transferred entry: ent-kaurenoic acid oxidase. Now EC 188.8.131.52, ent-kaurenoic acid oxidase (EC 184.108.40.206 created 2002, deleted 2018)]
[EC 220.127.116.11 Transferred entry: (R)-limonene 6-monooxygenase. Now classified as EC 18.104.22.168, (R)-limonene 6-monooxygenase (EC 22.214.171.124 created 2003, deleted 2017)]
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 126.96.36.199, 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
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]
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
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]
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 188.8.131.52, 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 184.108.40.206), C-11 (CobM; EC 220.127.116.11) and C-1 (CobF; EC 18.104.22.168) 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
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]
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 . In the absence of substrate, the enzyme can act as an NAD(P)H oxidase (EC 22.214.171.124).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 156621-13-5
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 126.96.36.199 Transferred entry: glyceollin synthase. Now EC 188.8.131.52, glyceollin synthase (EC 184.108.40.206 created 2004, deleted 2018)]
[EC 220.127.116.11 Deleted entry: 2-hydroxyisoflavanone synthase. This enzyme was classified on the basis of an incorrect reaction. The activity is covered by EC 18.104.22.168 2-hydroxyisoflavanone synthase (EC 22.214.171.124 created 2004, deleted 2013)]
[EC 126.96.36.199 Transferred entry: licodione synthase. Now EC 188.8.131.52, licodione synthase (EC 184.108.40.206 created 2004, deleted 2018)]
[EC 220.127.116.11 Transferred entry: flavanoid 3',5'-hydroxylase. Now EC 18.104.22.168, flavanoid 3',5'-hydroxylase (EC 22.214.171.124 created 2004, deleted 2018)]
[EC 126.96.36.199 Transferred entry: isoflavone 2-hydroxylase. Now EC 188.8.131.52, isoflavone 2-hydroxylase (EC 184.108.40.206 created 2005, deleted 2018)]
[EC 220.127.116.11 Transferred entry: zeaxanthin epoxidase. Now EC 18.104.22.168, zeaxanthin epoxidase (EC 22.214.171.124 created 2005, deleted 2016)]
[EC 126.96.36.199 Transferred entry: deoxysarpagine hydroxylase. Now EC 188.8.131.52, deoxysarpagine hydroxylase (EC 184.108.40.206 created 2005, deleted 2018)]
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
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 220.127.116.11 Transferred entry: (+)-abscisic acid 8-hydroxylase. Now EC 18.104.22.168, (+)-abscisic acid 8-hydroxylase (EC 22.214.171.124 created 2005, deleted 2018)]
[EC 126.96.36.199 Transferred entry: lithocholate 6β-hydroxylase. Now EC 188.8.131.52, lithocholate 6β-hydroxylase (EC 184.108.40.206 created 2005, deleted 2018)]
[EC 220.127.116.11 Transferred entry: 7α-hydroxycholest-4-en-3-one 12α-hydroxylase. Now EC 18.104.22.168, 7α-hydroxycholest-4-en-3-one 12α-hydroxylase (EC 22.214.171.124 created 2005, deleted 2015)]
[EC 126.96.36.199 Transferred entry: 5β-cholestane-3α,7α-diol 12α-hydroxylase. Now EC 188.8.131.52, 5β-cholestane-3α,7α-diol 12α-hydroxylase (EC 184.108.40.206 created 2005, deleted 2018)]
[EC 220.127.116.11 Transferred entry: taurochenodeoxycholate 6α-hydroxylase. Now EC 18.104.22.168, taurochenodeoxycholate 6α-hydroxylase (EC 22.214.171.124 created 2005, deleted 2018)]
[EC 126.96.36.199 Transferred entry: cholesterol 24-hydroxylase, Now EC 188.8.131.52, cholesterol 24-hydroxylase (EC 184.108.40.206 created 2005, deleted 2016)]
[EC 220.127.116.11 Transferred entry: 24-hydroxycholesterol 7α-hydroxylase, now classified as EC 18.104.22.168, 24-hydroxycholesterol 7α-hydroxylase (EC 22.214.171.124 created 2005, deleted 2016)]
[EC 126.96.36.199 Transferred entry: 25/26-hydroxycholesterol 7α-hydroxylase. Now classified as EC 188.8.131.52, 25/26-hydroxycholesterol 7α-hydroxylase (EC 184.108.40.206 created 2005, modified 2013 (EC 220.127.116.11 created 1999, incorporated 2013), deleted 2016)]