Continued from EC 1.14.13.1 to EC 1.14.13.50
EC 1.14.13.51 to EC 1.14.13.100
See also EC 1.14.13.151 to EC 1.14.13.252
EC 1.14.13.151 to EC 1.14.13.252
Accepted name: senecionine N-oxygenase
Reaction: senecionine + NADPH + H+ + O2 = senecionine N-oxide + NADP+ + H2O
Other name(s): senecionine monooxygenase (N-oxide-forming); SNO
Systematic name: senecionine,NADPH:oxygen oxidoreductase (N-oxide-forming)
Comments: A flavoprotein. NADH cannot replace NADPH. While pyrrolizidine alkaloids of the senecionine and monocrotaline types are generally good substrates (e.g. senecionine, retrorsine and monocrotaline), the enzyme does not use ester alkaloids lacking an hydroxy group at C-7 (e.g. supinine and phalaenopsine), 1,2-dihydro-alkaloids (e.g. sarracine) or unesterified necine bases (e.g. senkirkine) as substrates [1]. Senecionine N-oxide is used by insects as a chemical defense: senecionine N-oxide is non-toxic, but it is bioactivated to a toxic form by the action of cytochrome P-450 oxidase when absorbed by insectivores.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 220581-68-0
References:
1. Lindigkeit, R., Biller, A., Buch, M., Schiebel, H.M., Boppre, M. and Hartmann, T. The two facies of pyrrolizidine alkaloids: the role of the tertiary amine and its N-oxide in chemical defense of insects with acquired plant alkaloids. Eur. J. Biochem. 245 (1997) 626-636. [PMID: 9182998]
2. Naumann, C., Hartmann, T. and Ober, D. Evolutionary recruitment of a flavin-dependent monooxygenase for the detoxification of host plant-acquired pyrrolizidine alkaloids in the alkaloid-defended arctiid moth Tyria jacobaeae. Proc. Natl. Acad. Sci. USA 99 (2002) 6085-6090. [PMID: 11972041]
[EC 1.14.13.102 Transferred entry: psoralen synthase. Now EC 1.14.14.141, psoralen synthase (EC 1.14.13.102 created 2007, deleted 2018)]
[EC 1.14.13.103 Transferred entry: 8-dimethylallylnaringenin 2-hydroxylase. Now EC 1.14.14.142, 8-dimethylallylnaringenin 2-hydroxylase (EC 1.14.13.103 created 2007, deleted 2018)]
[EC 1.14.13.104 Transferred entry: (+)-menthofuran synthase. Now EC 1.14.14.143, (+)-menthofuran synthase (EC 1.14.13.104 created 2008, deleted 2018)]
Accepted name: monocyclic monoterpene ketone monooxygenase
Reaction: (1) (–)-menthone + NADPH + H+ + O2 = (4R,7S)-7-isopropyl-4-methyloxepan-2-one + NADP+ + H2O
(2) dihydrocarvone + NADPH + H+ + O2 = 4-isopropenyl-7-methyloxepan-2-one + NADP+ + H2O
(3) (iso)-dihydrocarvone + NADPH + H+ + O2 = 6-isopropenyl-3-methyloxepan-2-one + NADP+ + H2O
(4a) 1-hydroxymenth-8-en-2-one + NADPH + H+ + O2 = 7-hydroxy-4-isopropenyl-7-methyloxepan-2-one + NADP+ + H2O
(4b) 7-hydroxy-4-isopropenyl-7-methyloxepan-2-one = 3-isopropenyl-6-oxoheptanoate (spontaneous)
For diagram click here or click here or click here.
Other name(s): 1-hydroxy-2-oxolimonene 1,2-monooxygenase; dihydrocarvone 1,2-monooxygenase; MMKMO
Systematic name: (–)-menthone,NADPH:oxygen oxidoreductase
Comments: A flavoprotein (FAD). This Baeyer-Villiger monooxygenase enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 has wide substrate specificity, catalysing the lactonization of a large number of monocyclic monoterpene ketones and substituted cyclohexanones [2]. Both (1R,4S)- and (1S,4R)-1-hydroxymenth-8-en-2-one are metabolized, with the lactone product spontaneously rearranging to form 3-isopropenyl-6-oxoheptanoate [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. van der Werf, M.J., Swarts, H.J. and de Bont, J.A. Rhodococcus erythropolis DCL14 contains a novel degradation pathway for limonene. Appl. Environ. Microbiol. 65 (1999) 2092-2102. [PMID: 10224006]
2. Van Der Werf, M.J. Purification and characterization of a Baeyer-Villiger mono-oxygenase from Rhodococcus erythropolis DCL14 involved in three different monocyclic monoterpene degradation pathways. Biochem. J. 347 (2000) 693-701. [PMID: 10769172]
3. van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129-1141. [PMID: 10832640]
[EC 1.14.13.106 Transferred entry: epi-isozizaene 5-monooxygenase, now classified as EC 1.14.15.39, epi-isozizaene 5-monooxygenase. (EC 1.14.13.106 created 2008, deleted 2021)]
Accepted name: limonene 1,2-monooxygenase
Reaction: (1) (S)-limonene + NAD(P)H + H+ + O2 = 1,2-epoxymenth-8-ene + NAD(P)+ + H2O
(2) (R)-limonene + NAD(P)H + H+ + O2 = 1,2-epoxymenth-8-ene + NAD(P)+ + H2O
For diagram of reaction, click here
Glossary: limonene = mentha-1,8-diene
(S)-limonene = (–)-limonene
(R)-limonene = (+)-limonene
limonene-1,2-epoxide = 1,2-epoxymenth-8-ene = 1-methyl-4-(prop-1-en-2-yl)-7-oxabicyclo[4.1.0]heptane
Systematic name: limonene,NAD(P)H:oxygen oxidoreductase
Comments: A flavoprotein (FAD). Limonene is the most widespread terpene and is formed by more than 300 plants. Rhodococcus erythropolis DCL14, a Gram-positive bacterium, is able to grow on both (S)-limonene and (R)-limonene as the sole source of carbon and energy. NADPH can act instead of NADH, although more slowly. It has not been established if the product formed is optically pure or a mixture of two enantiomers.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. van der Werf, M.J., Swarts, H.J. and de Bont, J.A. Rhodococcus erythropolis DCL14 contains a novel degradation pathway for limonene. Appl. Environ. Microbiol. 65 (1999) 2092-2102. [PMID: 10224006]
[EC 1.14.13.108 Transferred entry: abieta-7,13-diene hydroxylase. Now EC 1.14.14.144, abieta-7,13-diene hydroxylase (EC 1.14.13.108 created 2009, modified 2012, deleted 2018)]
[EC 1.14.13.109 Transferred entry: abieta-7,13-dien-18-ol hydroxylase. Now EC 1.14.14.145, abieta-7,13-dien-18-ol hydroxylase (EC 1.14.13.109 created 2009, modified 2012, deleted 2018)]
[EC 1.14.13.110 Transferred entry: geranylgeraniol 18-hydroxylase. Now EC 1.14.14.146, geranylgeraniol 18-hydroxylase (EC 1.14.13.110 created 2009, deleted 2018)]
Accepted name: methanesulfonate monooxygenase (NADH)
Reaction: methanesulfonate + NADH + H+ + O2 = formaldehyde + NAD+ + sulfite + H2O
Glossary: methanesulfonate = CH3-SO3–
formaldehyde = H-CHO
Other name(s): mesylate monooxygenase; mesylate,reduced-FMN:oxygen oxidoreductase; MsmABC; methanesulfonic acid monooxygenase; MSA monooxygenase; MSAMO
Systematic name: methanesulfonate,NADH:oxygen oxidoreductase
Comments: A flavoprotein. Methanesulfonate is the simplest of the sulfonates and is a substrate for the growth of certain methylotrophic microorganisms. Compared with EC 1.14.14.5, alkanesulfonate monooxygenase, this enzyme has a restricted substrate range that includes only the short-chain aliphatic sulfonates (methanesulfonate to butanesulfonate) and excludes all larger molecules, such as arylsulfonates [1]. The enzyme from the bacterium Methylosulfonomonas methylovora is a multicomponent system comprising a hydroxylase, a reductase (MsmD) and a ferredoxin (MsmC). The hydroxylase has both large (MsmA) and small (MsmB) subunits, with each large subunit containing a Rieske-type [2Fe-2S] cluster. cf. EC 1.14.14.34, methanesulfonate monooxygenase (FMNH2).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. de Marco, P., Moradas-Ferreira, P., Higgins, T.P., McDonald, I., Kenna, E.M. and Murrell, J.C. Molecular analysis of a novel methanesulfonic acid monooxygenase from the methylotroph Methylosulfonomonas methylovora. J. Bacteriol. 181 (1999) 2244-2251. [PMID: 10094704]
2. Higgins, T.P., Davey, M., Trickett, J., Kelly, D.P. and Murrell, J.C. Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme. Microbiology 142 (1996) 251-260. [PMID: 8932698]
[EC 1.14.13.112 Transferred entry: 3-epi-6-deoxocathasterone 23-monooxygenase. Now EC 1.14.14.147, 3-epi-6-deoxocathasterone 23-monooxygenase (EC 1.14.13.112 created 2010, deleted 2018)]
Accepted name: FAD-dependent urate hydroxylase
Reaction: urate + NADH + H+ + O2 = 5-hydroxyisourate + NAD+ + H2O
Other name(s): HpxO enzyme; FAD-dependent urate oxidase; urate hydroxylase
Systematic name: urate,NADH:oxygen oxidoreductase (5-hydroxyisourate forming)
Comments: A flavoprotein. The reaction is part of the purine catabolic pathway in the bacterium Klebsiella pneumoniae. The enzyme is different from EC 1.7.3.3, factor-independent urate hydroxylase, found in most plants, which produces hydrogen peroxide. The product of the enzyme is a substrate for EC 3.5.2.17, hydroxyisourate hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. O'Leary, S.E., Hicks, K.A., Ealick, S.E. and Begley, T.P. Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase. Biochemistry 48 (2009) 3033-3035. [PMID: 19260710]
Accepted name: 6-hydroxynicotinate 3-monooxygenase
Reaction: 6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
Other name(s): NicC; 6HNA monooxygenase; HNA-3-monooxygenase
Systematic name: 6-hydroxynicotinate,NADH:oxygen oxidoreductase (3-hydroxylating, decarboxylating)
Comments: A flavoprotein (FAD) [1]. The reaction is involved in the aerobic catabolism of nicotinic acid.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Nakano, H., Wieser, M., Hurh, B., Kawai, T., Yoshida, T., Yamane, T. and Nagasawa, T. Purification, characterization and gene cloning of 6-hydroxynicotinate 3-monooxygenase from Pseudomonas fluorescens TN5. Eur. J. Biochem. 260 (1999) 120-126. [PMID: 10091591]
2. 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 1.14.13.115 Transferred entry: angelicin synthase. Now EC 1.14.14.148, angelicin synthase (EC 1.14.13.115 created 2010, deleted 2018)]
[EC 1.14.13.116 Transferred entry: geranylhydroquinone 3-hydroxylase. Now EC 1.14.14.174, geranylhydroquinone 3-hydroxylase. (EC 1.14.13.116 created 2010, deleted 2019)]
[EC 1.14.13.117 Transferred entry: isoleucine N-monooxygenase, Now EC 1.14.14.39, isoleucine N-monooxygenase (EC 1.14.13.117 created 2010, deleted 2017)]
[EC 1.14.13.118 Transferred entry: valine N-monooxygenase. Now EC 1.14.14.38, valine N-monooxygenase (EC 1.14.13.118 created 2010, deleted 2017)]
[EC 1.14.13.119 Transferred entry: 5-epiaristolochene 1,3-dihydroxylase. Now EC 1.14.14.149, 5-epiaristolochene 1,3-dihydroxylase (EC 1.14.13.119 created 2011, deleted 2018)]
[EC 1.14.13.120 Transferred entry: costunolide synthase. Now EC 1.14.14.150, costunolide synthase (EC 1.14.13.120 created 2011, deleted 2018)]
[EC 1.14.13.121 Transferred entry: premnaspirodiene oxygenase. Now EC 1.14.14.151, premnaspirodiene oxygenase (EC 1.14.13.121 created 2011, deleted 2018)]
Accepted name: chlorophyllide-a oxygenase
Reaction: chlorophyllide a + 2 O2 + 2 NADPH + 2 H+ = chlorophyllide b + 3 H2O + 2
NADP+ (overall reaction)
(1a) chlorophyllide a + O2 + NADPH + H+ = 71-hydroxychlorophyllide a + H2O + NADP+
(1b) 71-hydroxychlorophyllide a + O2 + NADPH + H+ = chlorophyllide b + 2 H2O + NADP+
For diagram of reaction click here.
Other name(s): chlorophyllide a oxygenase; chlorophyll-b synthase; CAO
Systematic name: chlorophyllide-a:oxygen 71-oxidoreductase
Comments: Chlorophyll b is required for the assembly of stable light-harvesting complexes (LHCs) in the chloroplast of green algae, cyanobacteria and plants [2,3]. Contains a mononuclear iron centre [3]. The enzyme catalyses two successive hydroxylations at the 7-methyl group of chlorophyllide a. The second step yields the aldehyde hydrate, which loses H2O spontaneously to form chlorophyllide b [2]. Chlorophyll a and protochlorophyllide a are not substrates [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 216503-73-0
References:
1. Espineda, C.E., Linford, A.S., Devine, D. and Brusslan, J.A. The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyll b synthesis in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 96 (1999) 10507-10511. [PMID: 10468639]
2. Oster, U., Tanaka, R., Tanaka, A. and Rüdiger, W. Cloning and functional expression of the gene encoding the key enzyme for chlorophyll b biosynthesis (CAO) from Arabidopsis thaliana. Plant J. 21 (2000) 305-310. [PMID: 10758481]
3. Eggink, L.L., LoBrutto, R., Brune, D.C., Brusslan, J., Yamasato, A., Tanaka, A. and Hoober, J.K. Synthesis of chlorophyll b: localization of chlorophyllide a oxygenase and discovery of a stable radical in the catalytic subunit. BMC Plant Biol. 4 (2004) 5. [PMID: 15086960]
4. Porra, R.J., Schafer, W., Cmiel, E., Katheder, I. and Scheer, H. The derivation of the formyl-group oxygen of chlorophyll b in higher plants from molecular oxygen. Achievement of high enrichment of the 7-formyl-group oxygen from 18O2 in greening maize leaves. Eur. J. Biochem. 219 (1994) 671-679. [PMID: 8307032]
[EC 1.14.13.123 Transferred entry: germacrene A hydroxylase. Now EC 1.14.14.95, germacrene A hydroxylase (EC 1.14.13.123 created 2011, deleted 2018)]
[EC 1.14.13.124 Transferred entry: phenylalanine N-monooxygenase, now classified as EC 1.14.14.40, phenylalanine N-monooxygenase (EC 1.14.13.124 created 2011, deleted 2017)]
[EC 1.14.13.125 Transferred entry: tryptophan N-monooxygenase. Now EC 1.14.14.156, tryptophan N-monooxygenase (EC 1.14.13.125 created 2011, deleted 2018)]
[EC 1.14.13.126 Transferred entry: vitamin D3 24-hydroxylase, now classified as EC 1.14.15.16, vitamin D3 24-hydroxylase (EC 1.14.13.126 created 2011, deleted 2016)]
Accepted name: 3-(3-hydroxyphenyl)propanoate hydroxylase
Reaction: (1) 3-(3-hydroxyphenyl)propanoate + NADH + H+ + O2 = 3-(2,3-dihydroxyphenyl)propanoate + H2O + NAD+
(2) (2E)-3-(3-hydroxyphenyl)prop-2-enoate + NADH + H+ + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + H2O + NAD+
Glossary: 3-hydroxycinnamate = 3-coumarate = 3-(3-hydroxyphenyl)prop-2-enoate
Other name(s): mhpA (gene name)
Systematic name: 3-(3-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase (2-hydroxylating)
Comments: A flavoprotein (FAD). This enzyme participates in a meta-cleavage pathway employed by the bacterium Escherichia coli for the degradation of various phenylpropanoid compounds.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Burlingame, R. and Chapman, P.J. Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli. J. Bacteriol. 155 (1983) 113-121. [PMID: 6345502]
2. Burlingame, R.P., Wyman, L. and Chapman, P.J. Isolation and characterization of Escherichia coli mutants defective for phenylpropionate degradation. J. Bacteriol. 168 (1986) 55-64. [PMID: 3531186]
3. Ferrández, A., García, J.L. and Díaz, E. Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12. J. Bacteriol. 179 (1997) 2573-2581. [PMID: 9098055]
4. 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]
Accepted name: 7-methylxanthine demethylase
Reaction: 7-methylxanthine + O2 + NAD(P)H + H+ = xanthine + NAD(P)+ + H2O + formaldehyde
Other name(s): ndmC (gene name)
Systematic name: 7-methylxanthine:oxygen oxidoreductase (demethylating)
Comments: A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida prefers NADH over NADPH. The enzyme is specific for 7-methylxanthine [2]. Forms part of the caffeine degradation pathway.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Summers, R.M., Louie, T.M., Yu, C.L. and Subramanian, M. Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source. Microbiology 157 (2011) 583-592. [PMID: 20966097]
2. Summers, R.M., Louie, T.M., Yu, C.L., Gakhar, L., Louie, K.C. and Subramanian, M. Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids. J. Bacteriol. 194 (2012) 2041Ð2049. [PMID: 22328667]
[EC 1.14.13.129 Transferred entry: β-carotene 3-hydroxylase. Now EC 1.14.15.24, β-carotene 3-hydroxylase. (EC 1.14.13.129 created 2011, deleted 2017)]
Accepted name: pyrrole-2-carboxylate monooxygenase
Reaction: pyrrole-2-carboxylate + NADH + H+ + O2 = 5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
Other name(s): pyrrole-2-carboxylate oxygenase
Systematic name: pyrrole-2-carboxylate,NADH:oxygen oxidoreductase (5-hydroxylating)
Comments: A flavoprotein (FAD). The enzyme initiates the degradation of pyrrole-2-carboxylate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hormann, K. and Andreesen, J.R. Purification and characterization of a pyrrole-2-carboxylate oxygenase from Arthrobacter strain Py1. Biol. Chem. Hoppe-Seyler 375 (1994) 211-218. [PMID: 8011178]
2. Becker, D., Schrader, T. and Andreesen, J.R. Two-component flavin-dependent pyrrole-2-carboxylate monooxygenase from Rhodococcus sp. Eur. J. Biochem. 249 (1997) 739-747. [PMID: 9395321]
Accepted name: dissimilatory dimethyl sulfide monooxygenase
Reaction: dimethyl sulfide + O2 + NADH + H+ = methanethiol + formaldehyde + NAD+ + H2O
For diagram of reaction click here.
Other name(s): dmoAB (gene names); dimethyl sulfide C-monooxygenase; dimethylsulfide monooxygenase (ambiguous); dimethyl sulfide monooxygenase (ambiguous)
Systematic name: dimethyl sulfide,NADH:oxygen oxidoreductase
Comments: The enzyme participates exclusively in sulfur dissimilation. It has lower activity with diethyl sulfide and other short-chain alkyl methyl sulfides. Its activity is stimulated by combined addition of FMN, and, after depletion of cations, of Mg2+ and Fe2+. The enzymes from bacteria of the Hyphomicrobium genus are a two component system that includes an FMN-dependent reductase subunit and a monooxygenase subunit.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. De Bont, J.A.M., Van Dijken, J.P. and Harder, W. Dimethyl sulphoxide and dimethyl sulphide as a carbon, sulphur and energy source for growth of Hyphomicrobium S. J. Gen. Microbiol. 127 (1981) 315-323.
2. Boden, R., Borodina, E., Wood, A.P., Kelly, D.P., Murrell, J.C. and Schafer, H. Purification and characterization of dimethylsulfide monooxygenase from Hyphomicrobium sulfonivorans. J. Bacteriol. 193 (2011) 1250-1258. [PMID: 21216999]
[EC 1.14.13.132 Transferred entry: squalene monooxygenase. Now EC 1.14.14.17, squalene monooxygenase (EC 1.14.13.132 created 1961 as EC 1.99.1.13, transferred 1965 to EC 1.14.1.3, part transferred 1972 to EC 1.14.99.7, transferred 2011 to EC 1.14.13.132, deleted 2015)]
[EC 1.14.13.133 Transferred entry: pentalenene oxygenase. Now EC 1.14.15.32, pentalenene oxygenase (EC 1.14.13.133 created 2011, deleted 2018)]
[EC 1.14.13.134 Transferred entry: β-amyrin 11-oxidase. Now EC 1.14.14.152, β-amyrin 11-oxidase (EC 1.14.13.134 created 2011, deleted 2018)]
Accepted name: 1-hydroxy-2-naphthoate hydroxylase
Reaction: 1-hydroxy-2-naphthoate + NAD(P)H + H+ + O2 = 1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2
Other name(s): 1-hydroxy-2-naphthoic acid hydroxylase
Systematic name: 1-hydroxy-2-naphthoate,NAD(P)H:oxygen oxidoreductase (2-hydroxylating, decarboxylating)
Comments: The enzyme is involved in the catabolic pathway for the degradation of chrysene in some bacteria [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Deveryshetty, J. and Phale, P.S. Biodegradation of phenanthrene by Alcaligenes sp. strain PPH: partial purification and characterization of 1-hydroxy-2-naphthoic acid hydroxylase. FEMS Microbiol. Lett. 311 (2010) 93-101. [PMID: 20727010]
2. Nayak, A.S., Sanjeev Kumar, S., Santosh Kumar, M., Anjaneya, O. and Karegoudar, T.B. A catabolic pathway for the degradation of chrysene by Pseudoxanthomonas sp. PNK-04. FEMS Microbiol. Lett. 320 (2011) 128-134. [PMID: 21545490]
[EC 1.14.13.136 Transferred entry: 2-hydroxyisoflavanone synthase. Now EC 1.14.14.87, 2-hydroxyisoflavanone synthase (EC 1.14.13.136 created 2011, modified 2013, deleted 2018)]
[EC 1.14.13.137 Transferred entry: indole-2-monooxygenase. Now EC 1.14.14.153, indole-2-monooxygenase (EC 1.14.13.137 created 2012, deleted 2018)]
[EC 1.14.13.138 Transferred entry: indolin-2-one monooxygenase. Now EC 1.14.14.157, indolin-2-one monooxygenase (EC 1.14.13.138 created 2012, deleted 2018)]
[EC 1.14.13.139 Transferred entry: 3-hydroxyindolin-2-one monooxygenase. Now EC 1.14.14.109, 3-hydroxyindolin-2-one monooxygenase (EC 1.14.13.139 created 2012, deleted 2018)]
[EC 1.14.13.140 Transferred entry: 2-hydroxy-1,4-benzoxazin-3-one monooxygenase. Now EC 1.14.14.110, 2-hydroxy-1,4-benzoxazin-3-one monooxygenase. (EC 1.14.13.140 created 2012, deleted 2018)]
[EC 1.14.13.141 Transferred entry: now EC 1.14.15.29 cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming] (EC 1.14.13.141 created 2012, modified 2016, deleted 2018)]
[EC 1.14.13.142 Transferred entry: 3-ketosteroid 9α-monooxygenase. Now EC 1.14.15.30, 3-ketosteroid 9α-monooxygenase (EC 1.14.13.142 created 2012, deleted 2018)]
[EC 1.14.13.143 Transferred entry: ent-isokaurene C2-hydroxylase. Now EC 1.14.14.76 ent-isokaurene C2/C3-hydroxylase (EC 1.14.13.143 created 2012, deleted 2018)]
[EC 1.14.13.144 Transferred entry: 9β-pimara-7,15-diene oxidase. Now EC 1.14.14.111, 9β-pimara-7,15-diene oxidase. (EC 1.14.13.144 created 2012, deleted 2018)]
[EC 1.14.13.145 Transferred entry: ent-cassa-12,15-diene 11-hydroxylase. Now EC 1.14.14.112, ent-cassa-12,15-diene 11-hydroxylase. (EC 1.14.13.145 created 2012, deleted 2018)]
Accepted name: taxoid 14β-hydroxylase
Reaction: 10β-hydroxytaxa-4(20),11-dien-5α-yl acetate + O2 + NADPH + H+ = 10β,14β-dihydroxytaxa-4(20),11-dien-5α-yl acetate + NADP+ + H2O
For diagram of reaction click here.
Systematic name: 10β-hydroxytaxa-4(20),11-dien-5α-yl-acetate,NADPH:oxygen 14-oxidoreductase
Comments: Requires cytochrome P450. From the yew Taxus cuspidata. Also acts on taxa-4(20),11-dien-5α-yl acetate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Jennewein, S., Rithner, C.D., Williams, R.M. and Croteau, R. Taxoid metabolism: taxoid 14β-hydroxylase is a cytochrome P450-dependent monooxygenase. Arch. Biochem. Biophys. 413 (2003) 262-270. [PMID: 12729625]
[EC 1.14.13.147 Transferred entry: taxoid 7β-hydroxylase. Now EC 1.14.14.182, taxoid 7β-hydroxylase (EC 1.14.13.147 created 2012, deleted 2022)]
Accepted name: trimethylamine monooxygenase
Reaction: N,N,N-trimethylamine + NADPH + H+ + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O
Other name(s): flavin-containing monooxygenase 3; FMO3; tmm (gene name)
Systematic name: N,N,N-trimethylamine,NADPH:oxygen oxidoreductase (N-oxide-forming)
Comments: A flavoprotein. The bacterial enzyme enables bacteria to use trimethylamine as the sole source of carbon and energy [1,4]. The mammalian enzyme is involved in detoxification of trimethylamine. Mutations in the human enzyme cause the inheritable disease known as trimethylaminuria (fish odor syndrome) [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Large, P.J., Boulton, C.A. and Crabbe, M.J. The reduced nicotinamide-adenine dinucleotide phosphate- and oxygen-dependent N-oxygenation of trimethylamine by Pseudomonas aminovorans. Biochem. J. 128 (1972) 137P-138P. [PMID: 4404764]
2. Dolphin, C.T., Riley, J.H., Smith, R.L., Shephard, E.A. and Phillips, I.R. Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA. Genomics 46 (1997) 260-267. [PMID: 9417913]
3. Treacy, E.P., Akerman, B.R., Chow, L.M., Youil, R., Bibeau, C., Lin, J., Bruce, A.G., Knight, M., Danks, D.M., Cashman, J.R. and Forrest, S.M. Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication. Hum. Mol. Genet. 7 (1998) 839-845. [PMID: 9536088]
4. Chen, Y., Patel, N.A., Crombie, A., Scrivens, J.H. and Murrell, J.C. Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase. Proc. Natl. Acad. Sci. USA 108 (2011) 17791-17796. [PMID: 22006322]
Accepted name: phenylacetyl-CoA 1,2-epoxidase
Reaction: phenylacetyl-CoA + NADPH + H+ + O2 = 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + NADP+ + H2O
For diagram of reaction click here.
Glossary: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA = 2-{7-oxabicyclo[4.1.0]hepta-2,4-dien-1-yl}acetyl-CoA
Other name(s): ring 1,2-phenylacetyl-CoA epoxidase; phenylacetyl-CoA monooxygenase; PaaAC; PaaABC(D)E
Systematic name: phenylacetyl-CoA:oxygen oxidoreductase (1,2-epoxidizing)
Comments: Part of the aerobic pathway of phenylacetate catabolism in Escherichia coli and Pseudomonas putida.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Teufel, R., Mascaraque, V., Ismail, W., Voss, M., Perera, J., Eisenreich, W., Haehnel, W. and Fuchs, G. Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc. Natl. Acad. Sci. USA 107 (2010) 14390-14395. [PMID: 20660314]
2. Grishin, A.M., Ajamian, E., Zhang, L. and Cygler, M. Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of the Escherichia coli phenylacetyl-coenzyme A oxygenase complex. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 (2010) 1045-1049. [PMID: 20823522]
3. Grishin, A.M., Ajamian, E., Tao, L., Zhang, L., Menard, R. and Cygler, M. Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex. J. Biol. Chem. 286 (2011) 10735-10743. [PMID: 21247899]
[EC 1.14.13.150 Transferred entry: α-humulene 10-hydroxylase. Now EC 1.14.14.113, α-humulene 10-hydroxylase. (EC 1.14.13.150 created 2012, deleted 2018)]