Enzyme Nomenclature

Continued from EC 1.14.13.1 to EC 1.14.13.50
EC 1.14.13.51 to EC 1.14.13.100
EC 1.14.13.101 to EC 1.14.13.150

EC 1.14.13 (Continued)

Contents

EC 1.14.13.151 transferred now EC 1.14.14.84
EC 1.14.13.152 transferred now EC 1.14.14.83
EC 1.14.13.153 (+)-sabinene 3-hydroxylase
EC 1.14.13.154 erythromycin 12-hydroxylase
EC 1.14.13.155 α-pinene monooxygenase
EC 1.14.13.156 1,8-cineole 2-endo-monooxygenase
EC 1.14.13.157 transferred now EC 1.14.14.56
EC 1.14.13.158 amorpha-4,11-diene 12-monooxygenase
EC 1.14.13.159 transferred now EC 1.14.14.24
EC 1.14.13.160 (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase
EC 1.14.13.161 (+)-camphor 6-exo-hydroxylase
EC 1.14.13.162 2,5-diketocamphane 1,2-monooxygenase
EC 1.14.13.164 transferred now EC 1.13.11.65
EC 1.14.13.163 6-hydroxy-3-succinoylpyridine 3-monooxygenase
EC 1.14.13.165 transferred, now EC 1.14.14.47
EC 1.14.13.166 4-nitrocatechol 4-monooxygenase
EC 1.14.13.167 4-nitrophenol 4-monooxygenase
EC 1.14.13.168 indole-3-pyruvate monooxygenase
EC 1.14.13.169 transferred now EC 1.14.18.5
EC 1.14.13.170 pentalenolactone D synthase
EC 1.14.13.171 neopentalenolactone D synthase
EC 1.14.13.172 salicylate 5-hydroxylase
EC 1.14.13.173 11-oxo-β-amyrin 30-oxidase
EC 1.14.13.174 averantin hydroxylase
EC 1.14.13.175 aflatoxin B synthase
EC 1.14.13.176 tryprostatin B 6-hydroxylase
EC 1.14.13.177 fumitremorgin C monooxygenase
EC 1.14.13.178 methylxanthine N1-demethylase
EC 1.14.13.179 methylxanthine N3-demethylase
EC 1.14.13.180 aklavinone 12-hydroxylase
EC 1.14.13.181 13-deoxydaunorubicin hydroxylase
EC 1.14.13.182 2-heptyl-3-hydroxy-4(1H)-quinolone synthase
EC 1.14.13.183 dammarenediol 12-hydroxylase
EC 1.14.13.184 protopanaxadiol 6-hydroxylase
EC 1.14.13.185 pikromycin synthase
EC 1.14.13.186 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase
EC 1.14.13.187 L-evernosamine nitrososynthase
EC 1.14.13.188 6-deoxyerythronolide B hydroxylase
EC 1.14.13.189 5-methyl-1-naphthoate 3-hydroxylase
EC 1.14.13.190 ferruginol synthase
EC 1.14.13.191 transferred now EC 1.14.14.70
EC 1.14.13.192 oryzalexin E synthase
EC 1.14.13.193 oryzalexin D synthase
EC 1.14.13.194 transferred now EC 1.14.14.78
EC 1.14.13.195 L-ornithine N5-monooxygenase (NADPH)
EC 1.14.13.196 L-ornithine N5-monooxygenase [NAD(P)H]
EC 1.14.13.197 dihydromonacolin L hydroxylase
EC 1.14.13.198 monacolin L hydroxylase
EC 1.14.13.199 transferred now EC 1.14.14.79
EC 1.14.13.200 tetracenomycin A2 monooxygenase-dioxygenase
EC 1.14.13.201 β-amyrin 28-monooxygenase
EC 1.14.13.202 methyl farnesoate epoxidase
EC 1.14.13.203 farnesoate epoxidase
EC 1.14.13.204 long-chain acyl-CoA ω-monooxygenase
EC 1.14.13.205 transferred now EC 1.14.14.80
EC 1.14.13.206 laurate 7-monooxygenase
EC 1.14.13.207 transferred now EC 1.14.14.31
EC 1.14.13.208 benzoyl-CoA 2,3-epoxidase
EC 1.14.13.209 salicyloyl-CoA 5-hydroxylase
EC 1.14.13.210 4-methyl-5-nitrocatechol 5-monooxygenase
EC 1.14.13.211 rifampicin monooxygenase
EC 1.14.13.212 1,3,7-trimethyluric acid 5-monooxygenase
EC 1.14.13.213 bursehernin 5'-monooxygenase
EC 1.14.13.214 (–)-4'-demethyl-deoxypodophyllotoxin 4-hydroxylase
EC 1.14.13.215 protoasukamycin 4-monooxygenase
EC 1.14.13.216 asperlicin C monooxygenase
EC 1.14.13.217 protodeoxyviolaceinate monooxygenase
EC 1.14.13.218 5-methylphenazine-1-carboxylate 1-monooxygenase
EC 1.14.13.219 resorcinol 4-hydroxylase (NADPH)
EC 1.14.13.220 resorcinol 4-hydroxylase (NADH)
EC 1.14.13.221 transferred now EC 1.14.15.28
EC 1.14.13.222 aurachin C monooxygenase/isomerase
EC 1.14.13.223 3-hydroxy-4-methylanthranilyl-[aryl-carrier protein] 5-monooxygenase
EC 1.14.13.224 violacein synthase
EC 1.14.13.225 F-actin monooxygenase
EC 1.14.13.226 acetone monooxygenase (methylacetate-forming)
EC 1.14.13.227 propane 2-monooxygenase
EC 1.14.13.228 jasmonic acid 12-hydroxylase
EC 1.14.13.229 tert-butyl alcohol monooxygenase
EC 1.14.13.230 butane monooxygenase (soluble)
EC 1.14.13.231 tetracycline 11a-monooxygenase
EC 1.14.13.232 6-methylpretetramide 4-monooxygenase
EC 1.14.13.233 4-hydroxy-6-methylpretetramide 12a-monooxygenase
EC 1.14.13.234 5a,11a-dehydrotetracycline 5-monooxygenase
EC 1.14.13.235 indole-3-acetate monooxygenase
EC 1.14.13.236 toluene 4-monooxygenase
EC 1.14.13.237 aliphatic glucosinolate S-oxygenase
EC 1.14.13.238 dimethylamine monooxygenase
EC 1.14.13.239 carnitine monooxygenase
EC 1.14.13.240 2-polyprenylphenol 6-hydroxylase
EC 1.14.13.241 5-pyridoxate monooxygenase
EC 1.14.13.242 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase
EC 1.14.13.243 toluene 2-monooxygenase
EC 1.14.13.244 phenol 2-monooxygenase (NADH)
EC 1.14.13.245 assimilatory dimethylsulfide S-monooxygenase

[EC 1.14.13.151 Transferred entry: linalool 8-monooxygenase. Now EC 1.14.14.84, linalool 8-monooxygenase (EC 1.14.13.151 created 1989 as EC 1.14.99.28, transferred 2012 to EC 1.14.13.151, deleted 2018)]

[EC 1.14.13.152 Transferred entry: geraniol 8-hydroxylase. Now EC 1.14.14.83, geraniol 8-hydroxylase (EC 1.14.13.152 created 2012, deleted 2018)]

EC 1.14.13.153

Accepted name: (+)-sabinene 3-hydroxylase

Reaction: (+)-sabinene + NADPH + H+ + O2 = (+)-cis-sabinol + NADP+ + H2O

For diagram of reaction click here.

Systematic name: (+)-sabinene,NADPH:oxygen oxidoreductase (3-hydroxylating)

Comments: Requires cytochrome P450. The enzyme has been characterized from Salvia officinalis (sage).

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

References:

1. Karp, F., Harris, J.L. and Croteau, R. Metabolism of monoterpenes: demonstration of the hydroxylation of (+)-sabinene to (+)-cis-sabinol by an enzyme preparation from sage (Salvia officinalis) leaves. Arch. Biochem. Biophys. 256 (1987) 179-193. [PMID: 3111374]

[EC 1.14.13.153 created 2012]

EC 1.14.13.154

Accepted name: erythromycin 12-hydroxylase

Reaction: erythromycin D + NADPH + H+ + O2 = erythromycin C + NADP+ + H2O

For diagram of reaction click here.

Other name(s): EryK

Systematic name: erythromycin-D,NADPH:oxygen oxidoreductase (12-hydroxylating)

Comments: The enzyme is responsible for the C-12 hydroxylation of the macrolactone ring, one of the last steps in erythromycin biosynthesis. It shows 1200-1900-fold preference for erythromycin D over the alternative substrate erythromycin B [1].

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

References:

1. Lambalot, R.H., Cane, D.E., Aparicio, J.J. and Katz, L. Overproduction and characterization of the erythromycin C-12 hydroxylase, EryK. Biochemistry 34 (1995) 1858-1866. [PMID: 7849045]

2. Savino, C., Montemiglio, L.C., Sciara, G., Miele, A.E., Kendrew, S.G., Jemth, P., Gianni, S. and Vallone, B. Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate. J. Biol. Chem. 284 (2009) 29170-29179. [PMID: 19625248]

3. Montemiglio, L.C., Gianni, S., Vallone, B. and Savino, C. Azole drugs trap cytochrome P450 EryK in alternative conformational states. Biochemistry 49 (2010) 9199-9206. [PMID: 20845962]

[EC 1.14.13.154 created 2012]

EC 1.14.13.155

Accepted name: α-pinene monooxygenase

Reaction: (–)-α-pinene + NADH + H+ + O2 = α-pinene oxide + NAD+ + H2O

For diagram of reaction click here.

Systematic name: (–)-α-pinene,NADH:oxygen oxidoreductase

Comments: Involved in the catabolism of α-pinene.

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

References:

1. Colocousi, A. Saqib, K.M. and Leak, D.J. Mutants of Pseudomonas fuorescence NCIMB 11671 defective in the catabolism of α-pinene. Appl. Microbiol. Biotechnol. 45 (1996) 822-830.

[EC 1.14.13.155 created 2012]

[EC 1.14.13.156 Transferred entry: 1,8-cineole 2-endo-monooxygenase. Now EC 1.14.14.133, 1,8-cineole 2-endo-monooxygenase (EC 1.14.13.156 created 2012, deleted 2018)]

[EC 1.14.13.157 Transferred entry: 1,8-cineole 2-exo-monooxygenase. Now EC 1.14.14.56, 1,8-cineole 2-exo-monooxygenase (EC 1.14.13.157 created 2012, deleted 2017)]

[EC 1.14.13.158 Transferred entry: amorpha-4,11-diene 12-monooxygenase. Now EC 1.14.14.114, amorpha-4,11-diene 12-monooxygenase. (EC 1.14.13.158 created 2012, deleted 2018)]

[EC 1.14.13.159 Transferred entry: vitamin D 25-hydroxylase, now classified as EC 1.14.14.24, vitamin D 25-hydroxylase (EC 1.14.13.159 created 2012, deleted 2016)]

EC 1.14.13.160

Accepted name: (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase

Reaction: [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA + O2 + NADPH + H+ = [(2R)-3,3,4-trimethyl-6-oxo-3,6-dihydro-1H-pyran-2-yl]acetyl-CoA + NADP+ + H2O

For diagram of reaction click here.

Glossary: (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA = 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA

Other name(s): 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase; 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA 1,2-monooxygenase; OTEMO

Systematic name: [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA,NADPH:oxygen oxidoreductase (1,5-lactonizing)

Comments: A FAD dependent enzyme isolated from Pseudomonas putida. Forms part of the catabolism pathway of camphor. It acts on the CoA ester in preference to the free acid.

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

References:

1. Ougham, H.J., Taylor, D.G. and Trudgill, P.W. Camphor revisited: involvement of a unique monooxygenase in metabolism of 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetic acid by Pseudomonas putida. J. Bacteriol. 153 (1983) 140-152. [PMID: 6848481]

2. Leisch, H., Shi, R., Grosse, S., Morley, K., Bergeron, H., Cygler, M., Iwaki, H., Hasegawa, Y. and Lau, P.C. Cloning, Baeyer-Villiger biooxidations, and structures of the camphor pathway 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-coenzyme A monooxygenase of Pseudomonas putida ATCC 17453. Appl. Environ. Microbiol. 78 (2012) 2200-2212. [PMID: 22267661]

3. Kadow, M., Loschinski, K., Sass, S., Schmidt, M. and Bornscheuer, U.T. Completing the series of BVMOs involved in camphor metabolism of Pseudomonas putida NCIMB 10007 by identification of the two missing genes, their functional expression in E. coli, and biochemical characterization. Appl. Microbiol. Biotechnol. (2012) . [PMID: 22286514]

[EC 1.14.13.160 created 2012]

EC 1.14.13.161

Accepted name: (+)-camphor 6-exo-hydroxylase

Reaction: (+)-camphor + NADPH + H+ + O2 = (+)-6-exo-hydroxycamphor + NADP+ + H2O

For diagram of reaction click here.

Other name(s): (+)-camphor 6-hydroxylase

Systematic name: (+)-camphor,NADPH:oxygen oxidoreductase (6-exo-hydroxylating)

Comments: A cytochrome P-450 monooxygenase isolated from Salvia officinalis (sage). Involved in the catabolism of camphor in senescent tissue.

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

References:

1. Funk, C., Koepp, A.E. and Croteau, R. Catabolism of camphor in tissue cultures and leaf disks of common sage (Salvia officinalis). Arch. Biochem. Biophys. 294 (1992) 306-313. [PMID: 1550356]

2. Funk, C. and Croteau, R. Induction and characterization of a cytochrome P-450-dependent camphor hydroxylase in tissue cultures of common sage (Salvia officinalis). Plant Physiol. 101 (1993) 1231-1237. [PMID: 12231778]

[EC 1.14.13.161 created 2012]

[EC 1.14.13.162 Transferred entry: 2,5-diketocamphane 1,2-monooxygenase. Now EC 1.14.14.108, 2,5-diketocamphane 1,2-monooxygenase (EC 1.14.13.162 created 1972 as EC 1.14.15.2, transferred 2012 to EC 1.14.13.162, deleted 2018)]

EC 1.14.13.163

Accepted name: 6-hydroxy-3-succinoylpyridine 3-monooxygenase

Reaction: 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O

Glossary: 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate = 6-hydroxy-3-succinoyl-pyridine

Other name(s): 6-hydroxy-3-succinoylpyridine hydroxylase; hspA (gene name); hspB (gene name)

Systematic name: 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate,NADH:oxygen oxidoreductase (3-hydroxylating, succinate semialdehyde releasing)

Comments: The enzyme catalyses a reaction in the nicotine degradation pathway of Pseudomonas species. One of the enzymes from the soil bacterium Pseudomonas putida S16 contains an FAD cofactor [2].

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

References:

1. Tang, H., Wang, S., Ma, L., Meng, X., Deng, Z., Zhang, D., Ma, C. and Xu, P. A novel gene, encoding 6-hydroxy-3-succinoylpyridine hydroxylase, involved in nicotine degradation by Pseudomonas putida strain S16. Appl. Environ. Microbiol. 74 (2008) 1567-1574. [PMID: 18203859]

2. Tang, H., Yao, Y., Zhang, D., Meng, X., Wang, L., Yu, H., Ma, L. and Xu, P. A novel NADH-dependent and FAD-containing hydroxylase is crucial for nicotine degradation by Pseudomonas putida. J. Biol. Chem. 286 (2011) 39179-39187. [PMID: 21949128]

[EC 1.14.13.163 created 2012]

[EC 1.14.13.164 Transferred entry: carotenoid isomerooxygenase. Now EC 1.13.11.65, carotenoid isomerooxygenase. The enzyme was discovered at the public-review stage to have been misclassified and so was withdrawn. (EC 1.14.13.164 created 2012, deleted 2012)]

[EC 1.14.13.165 Transferred entry: nitric-oxide synthase [NAD(P)H]. Now classified as EC 1.14.14.47, nitric-oxide synthase (flavodoxin) (EC 1.14.13.165 created 2012, deleted 2017)]

EC 1.14.13.166

Accepted name: 4-nitrocatechol 4-monooxygenase

Reaction: 4-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O

For diagram of reaction click here.

Systematic name: 4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming)

Comments: Contains FAD. The enzyme catalyses the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite. Forms a two-component system with a flavoprotein reductase [1]. The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyse EC 1.14.13.29, 4-nitrophenol 2-monooxygenase [1,2] while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyse EC 1.14.13.167, 4-nitrophenol 4-monooxygenase [3].

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

References:

1. Kadiyala, V. and Spain, J.C. A two-component monooxygenase catalyzes both the hydroxylation of p-nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in Bacillus sphaericus JS905. Appl. Environ. Microbiol. 64 (1998) 2479-2484. [PMID: 9647818]

2. Kitagawa, W., Kimura, N. and Kamagata, Y. A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101. J. Bacteriol. 186 (2004) 4894-4902. [PMID: 15262926]

3. Zhang, J.J., Liu, H., Xiao, Y., Zhang, X.E. and Zhou, N.Y. Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from Pseudomonas sp. strain WBC-3. J. Bacteriol. 191 (2009) 2703-2710. [PMID: 19218392]

[EC 1.14.13.166 created 2012]

EC 1.14.13.167

Accepted name: 4-nitrophenol 4-monooxygenase

Reaction: 4-nitrophenol + NADPH + H+ + O2 = 1,4-benzoquinone + nitrite + NADP+ + H2O

For diagram of reaction click here.

Other name(s): pnpA (gene name); pdcA (gene name)

Systematic name: 4-nitrophenol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming)

Comments: Contains FAD. The enzyme catalyses the first step in a degradation pathway for 4-nitrophenol, the oxidation of 4-nitrophenol at position 4 with the concomitant removal of the nitro group as nitrite. The enzyme from the bacterium Pseudomonas sp. strain WBC-3 also catalyses EC 1.14.13.166, 4-nitrocatechol 4-monooxygenase.

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

References:

1. Zhang, J.J., Liu, H., Xiao, Y., Zhang, X.E. and Zhou, N.Y. Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from Pseudomonas sp. strain WBC-3. J. Bacteriol. 191 (2009) 2703-2710. [PMID: 19218392]

[EC 1.14.13.167 created 2012]

EC 1.14.13.168

Accepted name: indole-3-pyruvate monooxygenase

Reaction: (indol-3-yl)pyruvate + NADPH + H+ + O2 = (indol-3-yl)acetate + NADP+ + H2O + CO2

For diagram of reaction click here.

Glossary: (indol-3-yl)pyruvate = 3-(1H-indol-3-yl)-2-oxopropanoate
(indol-3-yl)acetate = 2-(1H-indol-3-yl)acetate = indole-3-acetate

Other name(s): YUC2 (gene name); spi1 (gene name)

Systematic name: indole-3-pyruvate,NADPH:oxygen oxidoreductase (1-hydroxylating, decarboxylating)

Comments: This plant enzyme, along with EC 2.6.1.99 L-tryptophan—pyruvate aminotransferase, is responsible for the biosynthesis of the plant hormone indole-3-acetate from L-tryptophan.

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

References:

1. Mashiguchi, K., Tanaka, K., Sakai, T., Sugawara, S., Kawaide, H., Natsume, M., Hanada, A., Yaeno, T., Shirasu, K., Yao, H., McSteen, P., Zhao, Y., Hayashi, K., Kamiya, Y. and Kasahara, H. The main auxin biosynthesis pathway in Arabidopsis. Proc. Natl. Acad. Sci. USA 108 (2011) 18512-18517. [PMID: 22025724]

2. Zhao, Y. Auxin biosynthesis: a simple two-step pathway converts tryptophan to indole-3-acetic acid in plants. Mol. Plant 5 (2012) 334-338. [PMID: 22155950]

[EC 1.14.13.168 created 2012]

[EC 1.14.13.169 Transferred entry: sphinganine C4-monooxygenase. Now EC 1.14.18.5, sphingolipid C4-monooxygenase (EC 1.14.13.169 created 2012, deleted 2015)]

EC 1.14.13.170

Accepted name: pentalenolactone D synthase

Reaction: 1-deoxy-11-oxopentalenate + NADPH + H+ + O2 = pentalenolactone D + NADP+ + H2O

For diagram of reaction click here.

Glossary: 1-deoxy-11-oxopentalenate = (1S,3aR,5aS)-1,7,7-trimethyl-2-oxo-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
pentalenolactone D = (1S,4aR,6aS,9aR)-1,8,8-trimethyl-2-oxo-1,2,4,4a,6a,7,8,9-octahydropentaleno[1,6a-c]pyran-5-carboxylate

Other name(s): penE (gene name); pntE (gene name)

Systematic name: 1-deoxy-11-oxopentalenate,NADH:oxygen oxidoreductase (pentalenolactone-D forming)

Comments: A FAD-dependent oxygenase. Isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae. The ketone undergoes a biological Baeyer-Villiger reaction. Part of the pathway of pentalenolactone biosynthesis.

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

References:

1. Seo, M.J., Zhu, D., Endo, S., Ikeda, H. and Cane, D.E. Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the final steps of the biosynthesis of pentalenolactone and neopentalenolactone. Biochemistry 50 (2011) 1739-1754. [PMID: 21250661]

[EC 1.14.13.170 created 2012]

EC 1.14.13.171

Accepted name: neopentalenolactone D synthase

Reaction: 1-deoxy-11-oxopentalenate + NADPH + H+ + O2 = neopentalenolactone D + NADP+ + H2O

For diagram of reaction click here.

Glossary: 1-deoxy-11-oxopentalenate = (1S,3aR,5aS)-1,7,7-trimethyl-2-oxo-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
neopentalenolactone D = (1S,4aR,6aS)-1,7,7-trimethyl-3-oxo-4,4a,6a,7,8,9-hexahydro-3H-pentaleno[6a,1-c]pyran-5-carboxylate

Other name(s): ptlE (gene name)

Systematic name: 1-deoxy-11-oxopentalenate,NADH:oxygen oxidoreductase (neopentalenolactone-D forming)

Comments: A FAD-dependent oxygenase. Isolated from the bacterium Streptomyces avermitilis. The ketone undergoes a biological Baeyer-Villiger reaction.

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

References:

1. Seo, M.J., Zhu, D., Endo, S., Ikeda, H. and Cane, D.E. Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the final steps of the biosynthesis of pentalenolactone and neopentalenolactone. Biochemistry 50 (2011) 1739-1754. [PMID: 21250661]

[EC 1.14.13.171 created 2012]

EC 1.14.13.172

Accepted name: salicylate 5-hydroxylase

Reaction: salicylate + NADH + H+ + O2 = 2,5-dihydroxybenzoate + NAD+ + H2O

Glossary: 2,5-dihydroxybenzoate = gentisate

Other name(s): nagG (gene name); nagH (gene name)

Systematic name: salicylate,NADH:oxygen oxidoreductase (5-hydroxylating)

Comments: This enzyme, which was characterized from the bacterium Ralstonia sp. U2, comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.7, ferredoxin—NAD(P)+ reductase), an iron-sulfur oxygenase, and ferredoxin.

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

References:

1. Fuenmayor, S.L., Wild, M., Boyes, A.L. and Williams, P.A. A gene cluster encoding steps in conversion of naphthalene to gentisate in Pseudomonas sp. strain U2. J. Bacteriol. 180 (1998) 2522-2530. [PMID: 9573207]

[EC 1.14.13.172 created 2013]

[EC 1.14.13.173 Transferred entry: 11-oxo-β-amyrin 30-oxidase. Now EC 1.14.14.115, 11-oxo-β-amyrin 30-oxidase. (EC 1.14.13.173 created 2013, deleted 2018)]

[EC 1.14.13.174 Transferred entry: averantin hydroxylase. Now EC 1.14.14.116, averantin hydroxylase (EC 1.14.13.174 created 2013, deleted 2018)]

[EC 1.14.13.175 Transferred entry: aflatoxin B synthase. Now EC 1.14.14.117, aflatoxin B synthase (EC 1.14.13.175 created 2013, deleted 2018)]

[EC 1.14.13.176 Transferred entry: tryprostatin B 6-hydroxylase. Now EC 1.14.14.118, tryprostatin B 6-hydroxylase (EC 1.14.13.176 created 2013, deleted 2018)]

[EC 1.14.13.177 Transferred entry: fumitremorgin C monooxygenase. Now EC 1.14.14.119, fumitremorgin C monooxygenase (EC 1.14.13.177 created 2013, deleted 2018)]

EC 1.14.13.178

Accepted name: methylxanthine N1-demethylase

Reaction: (1) caffeine + O2 + NAD(P)H + H+ = theobromine + NAD(P)+ + H2O + formaldehyde
(2) theophylline + O2 + NAD(P)H + H+ = 3-methylxanthine + NAD(P)+ + H2O + formaldehyde
(3) paraxanthine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde

Glossary: caffeine = 1,3,7-trimethylxanthine
theobromine = 3,7-dimethylxanthine
theophylline = 1,3-dimethylxanthine
paraxanthine = 1,7-dimethylxanthine

Other name(s): ndmA (gene name)

Systematic name: caffeine:oxygen oxidoreductase (N1-demethylating)

Comments: A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.179, methylxanthine N3-demethylase, and has a 5-fold higher activity with NADH than with NADPH [2]. Also demethylate 1-methylxantine with lower efficiency. Forms part of the degradation pathway of methylxanthines.

Links to other databases: BRENDA, 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) 2041-2049. [PMID: 22328667]

[EC 1.14.13.178 created 2013]

EC 1.14.13.179

Accepted name: methylxanthine N3-demethylase

Reaction: (1) theobromine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde
(2) 3-methylxanthine + O2 + NAD(P)H + H+ = xanthine + NAD(P)+ + H2O + formaldehyde

Glossary: theobromine = 3,7-dimethylxanthine

Other name(s): ndmB (gene name)

Systematic name: theobromine:oxygen oxidoreductase (N3-demethylating)

Comments: A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.178, methylxanthine N1-demethylase, and has higher activity with NADH than with NADPH [1]. Also demethylates caffeine and theophylline with lower efficiency. Forms part of the degradation pathway of methylxanthines.

Links to other databases: BRENDA, 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) 2041-2049. [PMID: 22328667]

[EC 1.14.13.179 created 2013]

EC 1.14.13.180

Accepted name: aklavinone 12-hydroxylase

Reaction: aklavinone + NADPH + H+ + O2 = ε-rhodomycinone + NADP+ + H2O

For diagram of reaction click here.

Glossary: aklavinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
ε-rhodomycinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7,12-pentahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate

Other name(s): DnrF; RdmE; aklavinone 11-hydroxylase (incorrect)

Systematic name: aklavinone,NADPH:oxygen oxidoreductase (12-hydroxylating)

Comments: The enzymes from the Gram-positive bacteria Streptomyces peucetius and Streptomyces purpurascens participate in the biosynthesis of daunorubicin, doxorubicin and rhodomycins. The enzyme from Streptomyces purpurascens is an FAD monooxygenase.

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

References:

1. Filippini, S., Solinas, M.M., Breme, U., Schluter, M.B., Gabellini, D., Biamonti, G., Colombo, A.L. and Garofano, L. Streptomyces peucetius daunorubicin biosynthesis gene, dnrF: sequence and heterologous expression. Microbiology 141 (1995) 1007-1016. [PMID: 7773378]

2. Niemi, J., Wang, Y., Airas, K., Ylihonko, K., Hakala, J. and Mantsala, P. Characterization of aklavinone-11-hydroxylase from Streptomyces purpurascens. Biochim. Biophys. Acta 1430 (1999) 57-64. [PMID: 10082933]

[EC 1.14.13.180 created 2013]

EC 1.14.13.181

Accepted name: 13-deoxydaunorubicin hydroxylase

Reaction: (1) 13-deoxydaunorubicin + NADPH + H+ + O2 = 13-dihydrodaunorubicin + NADP+ + H2O
(2) 13-dihydrodaunorubicin + NADPH + H+ + O2 = daunorubicin + NADP+ + 2 H2O

For diagram of reaction click here.

Glossary: 13-dihydrodaunorubicin = daunorubicinol = (1S,3S)-3,5,12-trihydroxy-3-(1-hydroxyethyl)-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
13-deoxydaunorubicin = (1S,3S)-3-ethyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
daunorubicin = (1S,3S)-3-acetyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside

Other name(s): DoxA

Systematic name: 13-deoxydaunorubicin,NADPH:oxygen oxidoreductase (13-hydroxylating)

Comments: The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius show broad substrate specificity for structures based on an anthracycline aglycone, but have a strong preference for 4-methoxy anthracycline intermediates (13-deoxydaunorubicin and 13-dihydrodaunorubicin) over their 4-hydroxy analogues (13-deoxycarminomycin and 13-dihydrocarminomycin), as well as a preference for substrates hydroxylated at the C-13 rather than the C-14 position.

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

References:

1. Walczak, R.J., Dickens, M.L., Priestley, N.D. and Strohl, W.R. Purification, properties, and characterization of recombinant Streptomyces sp. strain C5 DoxA, a cytochrome P-450 catalyzing multiple steps in doxorubicin biosynthesis. J. Bacteriol. 181 (1999) 298-304. [PMID: 9864343]

2. Dickens, M.L., Priestley, N.D. and Strohl, W.R. In vivo and in vitro bioconversion of ε-rhodomycinone glycoside to doxorubicin: functions of DauP, DauK, and DoxA. J. Bacteriol. 179 (1997) 2641-2650. [PMID: 9098063]

[EC 1.14.13.181 created 2013]

EC 1.14.13.182

Accepted name: 2-heptyl-3-hydroxy-4(1H)-quinolone synthase

Reaction: 2-heptyl-4(1H)-quinolone + NADH + H+ + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O

Glossary: 2-heptyl-4(1H)-quinolone = 2-heptyl-4-hydroxyquinoline
2-heptyl-3-hydroxy-4(1H)-quinolone = 2-heptyl-3,4-dihydroxyquinoline

Other name(s): PqsH; 2-heptyl-3,4-dihydroxyquinoline synthase

Systematic name: 2-heptyl-4(1H)-quinolone,NADH:oxygen oxidoreductase (3-hydroxylating)

Comments: The enzyme from the bacterium Pseudomonas aeruginosa catalyses the terminal step in biosynthesis of the signal molecule 2-heptyl-3,4-dihydroxyquinoline that plays a role in regulation of virulence genes.

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

References:

1. Schertzer, J.W., Brown, S.A. and Whiteley, M. Oxygen levels rapidly modulate Pseudomonas aeruginosa social behaviours via substrate limitation of PqsH. Mol. Microbiol. 77 (2010) 1527-1538. [PMID: 20662781]

[EC 1.14.13.182 created 2013]

[EC 1.14.13.183 Transferred entry: dammarenediol 12-hydroxylase. Now EC 1.14.14.120, dammarenediol 12-hydroxylase (EC 1.14.13.183 created 2013, deleted 2018)]

[EC 1.14.13.184 Transferred entry: protopanaxadiol 6-hydroxylase. Now EC 1.14.14.121, protopanaxadiol 6-hydroxylase (EC 1.14.13.184 created 2013, deleted 2018)]

[EC 1.14.13.185 Transferred entry: pikromycin synthase. Now EC 1.14.15.33, pikromycin synthase (EC 1.14.13.185 created 2014, deleted 2018)]

[EC 1.14.13.186 Transferred entry: 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase. Now EC 1.14.15.34, 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase (EC 1.14.13.186 created 2014, deleted 2018)]

EC 1.14.13.187

Accepted name: L-evernosamine nitrososynthase

Reaction: dTDP-β-L-evernosamine + 2 NADPH + 2 H+ + 2 O2 = dTDP-2,3,6-trideoxy-3-C-methyl-4-O-methyl-3-nitroso-β-L-arabino-hexopyranose + 2 NADP+ + 3 H2O (overall reaction)
(1a) dTDP-β-L-evernosamine + NADPH + H+ + O2 = dTDP-N-hydroxy-β-L-evernosamine + NADP+ + H2O
(1b) dTDP-N-hydroxy-β-L-evernosamine + NADPH + H+ + O2 = dTDP-2,3,6-trideoxy-3-C-methyl-4-O-methyl-3-nitroso-β-L-arabino-hexopyranose + NADP+ + 2 H2O

Glossary: dTDP-β-L-evernosamine = dTDP-3-amino-2,3,6-trideoxy-3-C-methyl-4-O-methyl-β-L-arabino-hexopyranose
dTDP-β-L-evernitrose = dTDP-2,3,6-trideoxy-3-C-methyl-4-O-methyl-3-nitro-β-L-arabino-hexopyranose

Systematic name: dTDP-β-L-evernosamine,NADPH:oxygen oxidoreductase (N-hydroxylating)

Comments: Requires FAD. Isolated from the bacterium Micromonospora carbonacea var. africana. The nitroso group is probably spontaneously oxidized to a nitro group giving dTDP-β-L-evernitrose, which is involved in the biosynthesis of the antibiotic everninomycin. The reaction was studied using dTDP-β-L-4-epi-vancosamine (dTDP-4-O-desmethyl-β-L-evernitrosamine).

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

References:

1. Hu, Y., Al-Mestarihi, A., Grimes, C.L., Kahne, D. and Bachmann, B.O. A unifying nitrososynthase involved in nitrosugar biosynthesis. J. Am. Chem. Soc. 130 (2008) 15756-15757. [PMID: 18983146]

2. Vey, J.L., Al-Mestarihi, A., Hu, Y., Funk, M.A., Bachmann, B.O. and Iverson, T.M. Structure and mechanism of ORF36, an amino sugar oxidizing enzyme in everninomicin biosynthesis. Biochemistry 49 (2010) 9306-9317. [PMID: 20866105]

[EC 1.14.13.187 created 2014]

[EC 1.14.13.188 Transferred entry: 6-deoxyerythronolide B hydroxylase. Now EC 1.14.15.35, 6-deoxyerythronolide B hydroxylase (EC 1.14.13.188 created 2014, deleted 2018)]

EC 1.14.13.189

Accepted name: 5-methyl-1-naphthoate 3-hydroxylase

Reaction: 5-methyl-1-naphthoate + NADPH + H+ + O2 = 3-hydroxy-5-methyl-1-naphthoate + NADP+ + H2O

For diagram of reaction click here.

Other name(s): AziB1

Systematic name: 5-methyl-1-naphthoate,NADPH:oxygen oxidoreductase (3-hydroxylating)

Comments: The enzyme from the bacterium Streptomyces sahachiroi is involved in the biosynthesis of 3-methoxy-5-methyl-1-naphthoate, a component of of the the antitumor antibiotic azinomycin B.

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

References:

1. Ding, W., Deng, W., Tang, M., Zhang, Q., Tang, G., Bi, Y. and Liu, W. Biosynthesis of 3-methoxy-5-methyl naphthoic acid and its incorporation into the antitumor antibiotic azinomycin B. Mol. Biosyst. 6 (2010) 1071-1081. [PMID: 20485749]

[EC 1.14.13.189 created 2014]

EC 1.14.13.190

Accepted name: ferruginol synthase

Reaction: abieta-8,11,13-triene + NADPH + H+ + O2 = ferruginol + NADP+ + H2O

For diagram of reaction click here.

Glossary: ferruginol = abieta-8,11,13-trien-12-ol

Other name(s): miltiradiene oxidase (incorrect); CYP76AH1; miltiradiene,NADPH:oxygen oxidoreductase (ferruginol forming) (incorrect)

Systematic name: abietatriene,NADPH:oxygen oxidoreductase (ferruginol-forming)

Comments: The enzyme is found in some members of the Lamiaceae (mint family). The enzyme from Rosmarinus officinalis (rosemary) is involved in biosynthesis of carnosic acid, while the enzyme from the Chinese medicinal herb Salvia miltiorrhiza is involved in the biosynthesis of the tanshinones, abietane-type norditerpenoid naphthoquinones that are the main lipophilic bioactive components found in the plant.

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

References:

1. Guo, J., Zhou, Y.J., Hillwig, M.L., Shen, Y., Yang, L., Wang, Y., Zhang, X., Liu, W., Peters, R.J., Chen, X., Zhao, Z.K. and Huang, L. CYP76AH1 catalyzes turnover of miltiradiene in tanshinones biosynthesis and enables heterologous production of ferruginol in yeasts. Proc. Natl. Acad. Sci. USA 110 (2013) 12108-12113. [PMID: 23812755]

2. Zi, J. and Peters, R.J. Characterization of CYP76AH4 clarifies phenolic diterpenoid biosynthesis in the Lamiaceae. Org. Biomol. Chem. 11 (2013) 7650-7652. [PMID: 24108414]

3. Bozic, D., Papaefthimiou, D., Bruckner, K., de Vos, R.C., Tsoleridis, C.A., Katsarou, D., Papanikolaou, A., Pateraki, I., Chatzopoulou, F.M., Dimitriadou, E., Kostas, S., Manzano, D., Scheler, U., Ferrer, A., Tissier, A., Makris, A.M., Kampranis, S.C. and Kanellis, A.K. Towards elucidating carnosic acid biosynthesis in Lamiaceae: functional characterization of the three first steps of the pathway in Salvia fruticosa and Rosmarinus officinalis. PLoS One 10 (2015) e0124106. [PMID: 26020634]

[EC 1.14.13.190 created 2014, modified 2015]

[EC 1.14.13.191 Transferred entry: ent-sandaracopimaradiene 3-hydroxylase. Now EC 1.14.14.70, ent-sandaracopimaradiene 3-hydroxylase (EC 1.14.13.191 created 2014, deleted 2018)]

[EC 1.14.13.192 Transferred entry: oryzalexin E synthase. Now EC 1.14.14.122, oryzalexin E synthase (EC 1.14.13.192 created 2014, deleted 2018)]

[EC 1.14.13.193 Transferred entry: oryzalexin D synthase. Now EC 1.14.14.123, oryzalexin D synthase (EC 1.14.13.193 created 2014, deleted 2018)]

[EC 1.14.13.194 Transferred entry: phylloquinone ω-hydroxylase. Now EC 1.14.14.78, phylloquinone ω-hydroxylase (EC 1.14.13.194 created 2014, deleted 2018)]

EC 1.14.13.195

Accepted name: L-ornithine N5-monooxygenase (NADPH)

Reaction: L-ornithine + NADPH + H+ + O2 = N5-hydroxy-L-ornithine + NADP+ + H2O

Other name(s): CchB; ornithine hydroxylase; EtcB; PvdA; Af-OMO; dffA (gene name)

Systematic name: L-ornithine,NADPH:oxygen oxidoreductase (N5-hydroxylating)

Comments: A flavoprotein (FAD). The enzyme is involved in biosynthesis of N5-hydroxy-L-ornithine, N5-formyl-N5-hydroxy-L-ornithine or N5-acetyl-N5-hydroxy-L-ornithine. These nonproteinogenic amino acids are building blocks of siderophores produced by some bacteria (e.g. Streptomyces coelicolor, Saccharopolyspora erythraea and Pseudomonas aeruginosa). The enzyme is specific for NADPH. cf. EC 1.14.13.196, L-ornithine N5-monooxygenase [NAD(P)H].

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

References:

1. Ge, L. and Seah, S.Y. Heterologous expression, purification, and characterization of an L-ornithine N5-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa. J. Bacteriol. 188 (2006) 7205-7210. [PMID: 17015659]

2. Meneely, K.M. and Lamb, A.L. Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism. Biochemistry 46 (2007) 11930-11937. [PMID: 17900176]

3. Pohlmann, V. and Marahiel, M.A. δ-amino group hydroxylation of L-ornithine during coelichelin biosynthesis. Org. Biomol. Chem. 6 (2008) 1843-1848. [PMID: 18452021]

4. Robbel, L., Helmetag, V., Knappe, T.A. and Marahiel, M.A. Consecutive enzymatic modification of ornithine generates the hydroxamate moieties of the siderophore erythrochelin. Biochemistry 50 (2011) 6073-6080. [PMID: 21650455]

[EC 1.14.13.195 created 2014]

EC 1.14.13.196

Accepted name: L-ornithine N5-monooxygenase [NAD(P)H]

Reaction: L-ornithine + NAD(P)H + H+ + O2 = N5-hydroxy-L-ornithine + NAD(P)+ + H2O

Other name(s): SidA (ambiguous)

Systematic name: L-ornithine,NAD(P)H:oxygen oxidoreductase (N5-hydroxylating)

Comments: A flavoprotein (FAD). The enzyme from the pathogenic fungus Aspergillus fumigatus catalyses a step in the biosynthesis of the siderophores triacetylfusarinine and desferriferricrocin, while the enzyme from the bacterium Kutzneria sp. 744 is involved in the biosynthesis of piperazate, a building block of the kutzneride family of antifungal antibiotics. Activity of the fungal enzyme is higher with NADPH, due to the fact that following the reduction of the flavin, NADP+ (but not NAD+) stabilizes the C4a-hydroperoxyflavin intermediate that oxidizes the substrate [3]. cf. EC 1.14.13.195, L-ornithine N5-monooxygenase (NADPH).

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

References:

1. Chocklett, S.W. and Sobrado, P. Aspergillus fumigatus SidA is a highly specific ornithine hydroxylase with bound flavin cofactor. Biochemistry 49 (2010) 6777-6783. [PMID: 20614882]

2. Franceschini, S., Fedkenheuer, M., Vogelaar, N.J., Robinson, H.H., Sobrado, P. and Mattevi, A. Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases. Biochemistry 51 (2012) 7043-7045. [PMID: 22928747]

3. Romero, E., Fedkenheuer, M., Chocklett, S.W., Qi, J., Oppenheimer, M. and Sobrado, P. Dual role of NADP(H) in the reaction of a flavin dependent N-hydroxylating monooxygenase. Biochim. Biophys. Acta 1824 (2012) 850-857. [PMID: 22465572]

4. Neumann, C.S., Jiang, W., Heemstra, J.R., Jr., Gontang, E.A., Kolter, R. and Walsh, C.T. Biosynthesis of piperazic acid via N5-hydroxy-ornithine in Kutzneria spp. 744. Chembiochem 13 (2012) 972-976. [PMID: 22522643]

[EC 1.14.13.196 created 2014]

[EC 1.14.13.197 Transferred entry: dihydromonacolin L hydroxylase. Now EC 1.14.14.124, dihydromonacolin L hydroxylase (EC 1.14.13.197 created 2014, deleted 2018)]

[EC 1.14.13.198 Transferred entry: monacolin L hydroxylase. Now EC 1.14.14.125, monacolin L hydroxylase (EC 1.14.13.198 created 2014, deleted 2018)]

[EC 1.14.13.199 Transferred entry: docosahexaenoic acid ω-hydroxylase. Now EC 1.14.14.79, docosahexaenoic acid ω-hydroxylase (EC 1.14.13.199 created 2014, deleted 2018)]

EC 1.14.13.200

Accepted name: tetracenomycin A2 monooxygenase-dioxygenase

Reaction: tetracenomycin A2 + 2 O2 + 2 NAD(P)H + 2 H+ = tetracenomycin C + 2 NAD(P)+ + H2O

For diagram of reaction click here and for mechanism click here.

Glossary: tetracenomycin A2 = methyl 10,12-dihydroxy-3,8-dimethoxy-1-methyl-6,11-dioxo-6,11-dihydrotetracene-2-carboxylate
tetracenomycin C = methyl (6aR,7S,10aR)-6a,7,10a,12-tetrahydroxy-3,8-dimethoxy-1-methyl-6,10,11-trioxo-6,6a,7,10,10a,11-hexahydrotetracene-2-carboxylate

Other name(s): TcmG; ElmG; tetracenomycin A2,NAD(P)H:O2 oxidoreductase (tetracenomycin C forming)

Systematic name: tetracenomycin A2,NAD(P)H:oxygen oxidoreductase (tetracenomycin C forming)

Comments: Isolated from the bacterium Streptomyces glaucescens. The enzyme was also isolated from the bacterium Streptomyces olivaceus, where it acts on 8-demethyltetracenomycin A2 (tetracenomycin B2) as part of elloramycin biosynthesis. The reaction involves a monooxygenase reaction which is followed by a dioxygenase reaction giving a gem-diol and an epoxide. Water opens the epoxide giving two hydroxy groups. The gem-diol eliminates water to give a ketone which is then reduced to a hydroxy group.

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

References:

1. Shen, B. and Hutchinson, C.R. Triple hydroxylation of tetracenomycin A2 to tetracenomycin C in Streptomyces glaucescens. Overexpression of the tcmG gene in Streptomyces lividans and characterization of the tetracenomycin A2 oxygenase. J. Biol. Chem. 269 (1994) 30726-30733. [PMID: 7982994]

2. Rafanan, E.R., Jr., Hutchinson, C.R. and Shen, B. Triple hydroxylation of tetracenomycin A2 to tetracenomycin C involving two molecules of O2 and one molecule of H2O. Org. Lett. 2 (2000) 3225-3227. [PMID: 11009387]

3. Beynon, J., Rafanan, E.R., Jr., Shen, B. and Fisher, A.J. Crystallization and preliminary X-ray analysis of tetracenomycin A2 oxygenase: a flavoprotein hydroxylase involved in polyketide biosynthesis. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 1647-1651. [PMID: 11092935]

[EC 1.14.13.200 created 2014]

[EC 1.14.13.201 Transferred entry: β-amyrin 28-monooxygenase. Now EC 1.14.14.126, β-amyrin 28-monooxygenase (EC 1.14.13.201 created 2015, deleted 2018)]

[EC 1.14.13.202 Transferred entry: methyl farnesoate epoxidase. Now EC 1.14.14.127, methyl farnesoate epoxidase (EC 1.14.13.202 created 2015, deleted 2018)]

[EC 1.14.13.203 Transferred entry: farnesoate epoxidase. Now EC 1.14.14.128, farnesoate epoxidase (EC 1.14.13.203 created 2015, deleted 2018)]

[EC 1.14.13.204 Transferred entry: long-chain acyl-CoA ω-monooxygenase. Now EC 1.14.14.129, long-chain acyl-CoA ω-monooxygenase (EC 1.14.13.204 created 2015, deleted 2018)]

[EC 1.14.13.205 Transferred entry: long-chain fatty acid ω-monooxygenase. Now EC 1.14.14.80, long-chain fatty acid ω-monooxygenase (EC 1.14.13.205 created 2015, deleted 2018)]

[EC 1.14.13.206 Transferred entry: laurate 7-monooxygenase. Now EC 1.14.14.130, laurate 7-monooxygenase (EC 1.14.13.206 created 2015, deleted 2018)]

[EC 1.14.13.207 Transferred entry: ipsdienol synthase, now classified as EC 1.14.14.31, ipsdienol synthase (EC 1.14.13.207 created 2015, deleted 2016)]

EC 1.14.13.208

Accepted name: benzoyl-CoA 2,3-epoxidase

Reaction: benzoyl-CoA + NADPH + H+ + O2 = 2,3-epoxy-2,3-dihydrobenzoyl-CoA + NADP+ + H2O

For diagram of reaction click here.

Other name(s): benzoyl-CoA dioxygenase/reductase (incorrect); BoxBA; BoxA/BoxB system; benzoyl-CoA 2,3-dioxygenase (incorrect)

Systematic name: benzoyl-CoA,NADPH:oxygen oxidoreductase (2,3-epoxydizing)

Comments: The enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii. BoxB functions as the oxygenase part of benzoyl-CoA oxygenase in conjunction with BoxA, the reductase component, which upon binding of benzoyl-CoA, transfers two electrons to the ring in the course of monooxygenation. BoxA is a homodimeric 46 kDa iron-sulfur-flavoprotein (FAD), BoxB is a monomeric iron-protein [1].

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

References:

1. Zaar, A., Gescher, J., Eisenreich, W., Bacher, A. and Fuchs, G. New enzymes involved in aerobic benzoate metabolism in Azoarcus evansii. Mol. Microbiol. 54 (2004) 223-238. [PMID: 15458418]

2. Gescher, J., Zaar, A., Mohamed, M., Schagger, H. and Fuchs, G. Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus evansii. J. Bacteriol. 184 (2002) 6301-6315. [PMID: 12399500]

3. Mohamed, M.E., Zaar, A., Ebenau-Jehle, C. and Fuchs, G. Reinvestigation of a new type of aerobic benzoate metabolism in the proteobacterium Azoarcus evansii. J. Bacteriol. 183 (2001) 1899-1908. [PMID: 11222587]

4. Rather, L.J., Knapp, B., Haehnel, W. and Fuchs, G. Coenzyme A-dependent aerobic metabolism of benzoate via epoxide formation. J. Biol. Chem. 285 (2010) 20615-20624. [PMID: 20452977]

[EC 1.14.13.208 created 2010 as EC 1.14.12.21, transferred 2015 to EC 1.14.13.208]

EC 1.14.13.209

Accepted name: salicyloyl-CoA 5-hydroxylase

Reaction: 2-hydroxybenzoyl-CoA + NADH + H+ + O2 = gentisyl-CoA + NAD+ + H2O

Glossary: 2-hydroxybenzoyl-CoA = salicyloyl-CoA
gentisate = 2,5-dihydroxybenzoate

Other name(s): sdgC (gene name)

Systematic name: salicyloyl-CoA,NADH:oxygen oxidoreductase (5-hydroxylating)

Comments: The enzyme, characterized from the bacterium Streptomyces sp. WA46, participates in a pathway for salicylate degradation. cf. EC 1.14.13.172, salicylate 5-hydroxylase.

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

References:

1. Ishiyama, D., Vujaklija, D. and Davies, J. Novel pathway of salicylate degradation by Streptomyces sp. strain WA46. Appl. Environ. Microbiol. 70 (2004) 1297-1306. [PMID: 15006746]

[EC 1.14.13.209 created 2015]

EC 1.14.13.210

Accepted name: 4-methyl-5-nitrocatechol 5-monooxygenase

Reaction: 4-methyl-5-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-5-methylquinone + nitrite + NAD(P)+ + H2O

Other name(s): dntB (gene name); 4-methyl-5-nitrocatechol oxygenase; MNC monooxygenase

Systematic name: 4-methyl-5-nitrocatechol,NAD(P)H:oxygen 5-oxidoreductase (5-hydroxylating, nitrite-forming)

Comments: Contains FAD. The enzyme, isolated from the bacterium Burkholderia sp. DNT, can use both NADH and NADPH, but prefers NADPH. It has a narrow substrate range, but can also act on 4-nitrocatechol.

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

References:

1. Haigler, B.E., Suen, W.C. and Spain, J.C. Purification and sequence analysis of 4-methyl-5-nitrocatechol oxygenase from Burkholderia sp. strain DNT. J. Bacteriol. 178 (1996) 6019-6024. [PMID: 8830701]

2. Leungsakul, T., Johnson, G.R. and Wood, T.K. Protein engineering of the 4-methyl-5-nitrocatechol monooxygenase from Burkholderia sp. strain DNT for enhanced degradation of nitroaromatics. Appl. Environ. Microbiol. 72 (2006) 3933-3939. [PMID: 16751499]

[EC 1.14.13.210 created 2016]

EC 1.14.13.211

Accepted name: rifampicin monooxygenase

Reaction: rifampicin + NAD(P)H + O2 = 2'-N-hydroxyrifampicin + NAD(P)+ + H2O

Glossary: rifampicin = (2S,12Z,14E,16S,17S,18R,19R,20R,21S,22R,23S,24E)-5,6,9,17,19-pentahydroxy-23-methoxy-2,4,12,16,18,20,22-heptamethyl-8-{[(E)-(4-methylpiperazin-1-yl)imino]methyl}-1,11-dioxo-1,2-dihydro-2,7-(epoxypentadeca-1,11,13-trienoimino)nathpho[2,1-b]furan-21-yl acetate

Other name(s): RIF-O

Systematic name: rifampicin:NAD(P)H:oxygen oxidoreductase (2'-N-hydroxyrifampicin-forming)

Comments: The enzyme has been found in the Corynebacteria Rhodococcus equi and Nocardia farcinica. It confers increased resistance to the antibiotic rifampicin by initiating its degradation.

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

References:

1. Andersen, S.J., Quan, S., Gowan, B. and Dabbs, E.R. Monooxygenase-like sequence of a Rhodococcus equi gene conferring increased resistance to rifampin by inactivating this antibiotic. Antimicrob. Agents Chemother. 41 (1997) 218-221. [PMID: 8980786]

2. Hoshino, Y., Fujii, S., Shinonaga, H., Arai, K., Saito, F., Fukai, T., Satoh, H., Miyazaki, Y. and Ishikawa, J. Monooxygenation of rifampicin catalyzed by the rox gene product of Nocardia farcinica: structure elucidation, gene identification and role in drug resistance. J. Antibiot. (Tokyo) 63 (2010) 23-28. [PMID: 19942945]

[EC 1.14.13.211 created 2016]

EC 1.14.13.212

Accepted name: 1,3,7-trimethyluric acid 5-monooxygenase

Reaction: 1,3,7-trimethylurate + NADH + H+ + O2 = 1,3,7-trimethyl-5-hydroxyisourate + NAD+ + H2O

Glossary: isourate = 1,3,5,7-tetrahydropurine-2,6,8-trione

Other name(s): tmuM (gene name)

Systematic name: 1,3,7-trimethylurate,NADH:oxygen oxidoreductase (1,3,7-trimethyl-5-hydroxyisourate forming)

Comments: The enzyme, characterized from the bacterium Pseudomonas sp. CBB1, is part of the bacterial C-8 oxidation-based caffeine degradation pathway. The product decomposes spontaneously to a racemic mixture of 3,6,8-trimethylallantoin. The enzyme shows no acitivity with urate. cf. EC 1.14.13.113, FAD-dependent urate hydroxylase.

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

References:

1. Mohanty, S.K., Yu, C.L., Das, S., Louie, T.M., Gakhar, L. and Subramanian, M. Delineation of the caffeine C-8 oxidation pathway in Pseudomonas sp. strain CBB1 via characterization of a new trimethyluric acid monooxygenase and genes involved in trimethyluric acid metabolism. J. Bacteriol. 194 (2012) 3872-3882. [PMID: 22609920]

2. Summers, R.M., Mohanty, S.K., Gopishetty, S. and Subramanian, M. Genetic characterization of caffeine degradation by bacteria and its potential applications. Microb Biotechnol 8 (2015) 369-378. [PMID: 25678373]

[EC 1.14.13.212 created 2016]

[EC 1.14.13.213 Transferred entry: bursehernin 5-monooxygenase. Now EC 1.14.14.131, bursehernin 5-monooxygenase (EC 1.14.13.213 created 2016, deleted 2018)]

[EC 1.14.13.214 Transferred entry: (ndash)-4'-demethyl-deoxypodophyllotoxin 4-hydroxylase. Now EC 1.14.14.132, (ndash)-4'-demethyl-deoxypodophyllotoxin 4-hydroxylase (EC 1.14.13.214 created 2016, deleted 2018)]

EC 1.14.13.215

Accepted name: protoasukamycin 4-monooxygenase

Reaction: protoasukamycin + NADH + H+ + O2 = 4-hydroxyprotoasukamycin + NAD+ + H2O

Glossary: asuE1 (gene name)

Systematic name: protoasukamycin,NADH:oxygen oxidoreductase (4-hydroxylating)

Comments: The enzyme, characterized from the bacterium Streptomyces nodosus subsp. asukaensis, is involved in the biosynthesis of the antibiotic asukamycin. Requires a flavin cofactor, with no preference among FMN, FAD or riboflavin. When flavin concentration is low, activity is enhanced by the presence of the NADH-dependent flavin-reductase AsuE2.

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

References:

1. Rui, Z., Sandy, M., Jung, B. and Zhang, W. Tandem enzymatic oxygenations in biosynthesis of epoxyquinone pharmacophore of manumycin-type metabolites. Chem. Biol. 20 (2013) 879-887. [PMID: 23890006]

[EC 1.14.13.215 created 2016]

EC 1.14.13.216

Accepted name: asperlicin C monooxygenase

Reaction: asperlicin C + NAD(P)H + H+ + O2 = asperlicin E + NAD(P)+ + H2O

Other name(s): AspB

Systematic name: asperlicin C,NAD(P)H:oxygen oxidoreductase

Comments: The enzyme, characterized from the fungus Aspergillus alliaceus, contains an FAD cofactor. The enzyme inserts a hydroxyl group, leading to formation of a N-C bond that creates an additional cycle between the bicyclic indole and the tetracyclic core moieties, resulting in the heptacyclic asperlicin E.

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

References:

1. Haynes, S.W., Gao, X., Tang, Y. and Walsh, C.T. Assembly of asperlicin peptidyl alkaloids from anthranilate and tryptophan: a two-enzyme pathway generates heptacyclic scaffold complexity in asperlicin E. J. Am. Chem. Soc. 134 (2012) 17444-17447. [PMID: 23030663]

[EC 1.14.13.216 created 2016]

EC 1.14.13.217

Accepted name: protodeoxyviolaceinate monooxygenase

Reaction: protodeoxyviolaceinate + NAD(P)H + O2 = protoviolaceinate + NAD(P)+ + H2O

For diagram of reaction click here.

Glossary: protodeoxyviolaceinate = 3,5-di(1H-indol-3-yl)-1H-pyrrole-2-carboxylate
protoviolaceinate = 5-(5-hydroxy-1H-indol-3-yl)-3-(1H-indol-3-yl)-1H-pyrrole-2-carboxylate

Other name(s): vioD (gene name); protoviolaceinate synthase

Systematic name: protodeoxyviolaceinate,NAD(P)H:O2 oxidoreductase

Comments: The enzyme, characterized from the bacterium Chromobacterium violaceum, participates in the biosynthesis of the violet pigment violacein. The product, protoviolaceinate, can be acted upon by EC 1.14.13.224, violacein synthase, leading to violacein production. However, it is very labile, and in the presence of oxygen can undergo non-enzymic autooxidation to the shunt product proviolacein.

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

References:

1. Balibar, C.J. and Walsh, C.T. In vitro biosynthesis of violacein from L-tryptophan by the enzymes VioA-E from Chromobacterium violaceum. Biochemistry 45 (2006) 15444-15457. [PMID: 17176066]

2. Shinoda, K., Hasegawa, T., Sato, H., Shinozaki, M., Kuramoto, H., Takamiya, Y., Sato, T., Nikaidou, N., Watanabe, T. and Hoshino, T. Biosynthesis of violacein: a genuine intermediate, protoviolaceinic acid, produced by VioABDE, and insight into VioC function. Chem. Commun. (Camb.) (2007) 4140-4142. [PMID: 17925955]

[EC 1.14.13.217 created 2016, modified 2016]

EC 1.14.13.218

Accepted name: 5-methylphenazine-1-carboxylate 1-monooxygenase

Reaction: 5-methylphenazine-1-carboxylate + NADH + O2 = pyocyanin + NAD+ + CO2 + H2O

For diagram of reaction click here.

Glossary: pyocyanin = 6-methylphenazin-6-ium-1-olate

Other name(s): phzS (gene name)

Systematic name: 5-methylphenazine-1-carboxylate,NADH:oxygen oxidoreductase (1-hydroxylating, decarboxylating)

Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanin, a toxin produced and secreted by the organism. It can also act on phenazine-1-carboxylate, converting it into 1-hydroxyphenazine.

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

References:

1. Mavrodi, D.V., Bonsall, R.F., Delaney, S.M., Soule, M.J., Phillips, G. and Thomashow, L.S. Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1. J. Bacteriol. 183 (2001) 6454-6465. [PMID: 11591691]

2. Parsons, J.F., Greenhagen, B.T., Shi, K., Calabrese, K., Robinson, H. and Ladner, J.E. Structural and functional analysis of the pyocyanin biosynthetic protein PhzM from Pseudomonas aeruginosa. Biochemistry 46 (2007) 1821-1828. [PMID: 17253782]

3. Greenhagen, B.T., Shi, K., Robinson, H., Gamage, S., Bera, A.K., Ladner, J.E. and Parsons, J.F. Crystal structure of the pyocyanin biosynthetic protein PhzS. Biochemistry 47 (2008) 5281-5289. [PMID: 18416536]

[EC 1.14.13.218 created 2016]

EC 1.14.13.219

Accepted name: resorcinol 4-hydroxylase (NADPH)

Reaction: resorcinol + NADPH + H+ + O2 = hydroxyquinol + NADP+ + H2O

Glossary: resorcinol = 1,3-dihydroxybenzene
hydroxyquinol = 1,2,4-trihydroxybenzene

Systematic name: resorcinol,NADPH:oxygen oxidoreductase (4-hydroxylating)

Comments: The enzyme, characterized from the bacterium Corynebacterium glutamicum, is a single-component hydroxylase. The enzyme has no activity with NADH. cf. EC 1.14.13.220, resorcinol 4-hydroxylase (NADH), and EC 1.14.14.27, resorcinol 4-hydroxylase (FADH2).

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

References:

1. Huang, Y., Zhao, K.X., Shen, X.H., Chaudhry, M.T., Jiang, C.Y. and Liu, S.J. Genetic characterization of the resorcinol catabolic pathway in Corynebacterium glutamicum. Appl. Environ. Microbiol. 72 (2006) 7238-7245. [PMID: 16963551]

[EC 1.14.13.219 created 2016]

EC 1.14.13.220

Accepted name: resorcinol 4-hydroxylase (NADH)

Reaction: resorcinol + NADH + H+ + O2 = hydroxyquinol + NAD+ + H2O

Glossary: resorcinol = 1,3-dihydroxybenzene
hydroxyquinol = 1,2,4-trihydroxybenzene

Other name(s): tsdB (gene name)

Systematic name: resorcinol,NADH:oxygen oxidoreductase (4-hydroxylating)

Comments: The enzyme, characterized from the bacterium Rhodococcus jostii RHA1, is a single-component hydroxylase. The enzyme has no activity with NADPH. cf. EC 1.14.13.219, resorcinol 4-hydroxylase (NADPH), and EC 1.14.14.27, resorcinol 4-hydroxylase (FADH2).

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

References:

1. Kasai, D., Araki, N., Motoi, K., Yoshikawa, S., Iino, T., Imai, S., Masai, E. and Fukuda, M. γ-Resorcylate catabolic-pathway genes in the soil actinomycete Rhodococcus jostii RHA1. Appl. Environ. Microbiol. 81 (2015) 7656-7665. [PMID: 26319878]

[EC 1.14.13.220 created 2016]

[EC 1.14.13.221 Transferred entry: cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]. Now EC 1.14.15.28, cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] (EC 1.14.13.221 created 2016, deleted 2018)]

EC 1.14.13.222

Accepted name: aurachin C monooxygenase/isomerase

Reaction: aurachin C + NAD(P)H + H+ + O2 = 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD(P)+ + H2O (overall reaction)
(1a) aurachin C + NAD(P)H + H+ + O2 = 2-hydroxy-1a-methyl-7a-[(2E,6E)-farnesyl]-1a,2-dihydrooxireno[2,3-b]quinolin-7(7aH)-one + NAD(P)+ + H2O
(1b) 2-hydroxy-1a-methyl-7a-[(2E,6E)-farnesyl]-1a,2-dihydrooxireno[2,3-b]quinolin-7(7aH)-one = 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide

For diagram of reaction click here and for mechanism click here.

Glossary: aurachin C = 1-hydroxy-2-methyl-3-[(2E,6E)-farnesyl]-4(1H)-quinolinone
2-hydroxy-1a-methyl-7a-[(2E,6E)-farnesyl]-1a,2-dihydrooxireno[2,3-b]quinolin-7(7aH)-one = 2-hydroxy-1a-methyl-7a-((2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl)-1a,2-dihydrooxireno[2,3-b]quinolin-7(7aH)-one
4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide = 4-hydroxy-2-methyl-4-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]quinolin-3(4H)-one 1-oxide
aurachin B = 2-methyl-4-[(2E,6E)-farnesyl]-3-quinolinol 1-oxide

Other name(s): auaG (gene name); aurachin C monooxygenase

Systematic name: aurachin C:NAD(P)H:oxygen oxidoreductase (4-hydroxy-2-methyl-3-oxo-4-farnesyl-3,4-dihydroquinoline-1-oxide-forming)

Comments: The aurachin C monooxygenase from the bacterium Stigmatella aurantiaca accepts both NADH and NADPH as cofactor, but has a preference for NADH. It catalyses the initial steps in the conversion of aurachin C to aurachin B. The FAD-dependent monooxygenase catalyses the epoxidation of the C2-C3 double bond of aurachin C, which is followed by a semipinacol rearrangement, causing migration of the farnesyl group from C3 to C4.

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

References:

1. Katsuyama, Y., Harmrolfs, K., Pistorius, D., Li, Y. and Muller, R. A semipinacol rearrangement directed by an enzymatic system featuring dual-function FAD-dependent monooxygenase. Angew Chem Int Ed Engl 51 (2012) 9437-9440. [PMID: 22907798]

[EC 1.14.13.222 created 2016]

EC 1.14.13.223

Accepted name: 3-hydroxy-4-methylanthranilyl-[aryl-carrier protein] 5-monooxygenase

Reaction: 3-hydroxy-4-methylanthranilyl-[aryl-carrier protein] + NADH + H+ + O2 = 3,5-dihydroxy-4-methylanthranilyl-[aryl-carrier protein] + NAD+ + H2O

Other name(s): sibG (gene name)

Systematic name: 3-hydroxy-4-methylanthranilyl-[aryl-carrier protein],NADH:oxygen oxidoreductase (5-hydroxylating)

Comments: A flavoprotein (FAD). The enzyme, characterized from the bacterium Streptosporangium sibiricum, is involved in the biosynthesis of the antitumor antibiotic sibiromycin. The enzyme is not active with free 3-hydroxy-4-methylanthranilate.

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

References:

1. Giessen, T.W., Kraas, F.I. and Marahiel, M.A. A four-enzyme pathway for 3,5-dihydroxy-4-methylanthranilic acid formation and incorporation into the antitumor antibiotic sibiromycin. Biochemistry 50 (2011) 5680-5692. [PMID: 21612226]

[EC 1.14.13.223 created 2016]

EC 1.14.13.224

Accepted name: violacein synthase

Reaction: (1) protoviolaceinate + NAD(P)H + O2 = violaceinate + NAD(P)+ + H2O
(2) protodeoxyviolaceinate + NAD(P)H + O2 = deoxyviolaceinate + NAD(P)+ + H2O

For diagram of reaction click here.

Glossary: violacein = 5-(5-hydroxy-3-indolyl)-3-(3-oxinodolylidene)-2-oxopyrroline

Other name(s): proviolaceinate monooxygenase; vioC (gene name)

Systematic name: protoviolaceinate,NAD(P)H:O2 oxidoreductase

Comments: The enzyme, characterized from the bacterium Chromobacterium violaceum, participates in the biosynthesis of the violet pigment violacein. The products, violaceinate and deoxyviolaceinate, undergo non-enzymic autooxidation into violacein and deoxyviolacein, respectively.

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

References:

1. Balibar, C.J. and Walsh, C.T. In vitro biosynthesis of violacein from L-tryptophan by the enzymes VioA-E from Chromobacterium violaceum. Biochemistry 45 (2006) 15444-15457. [PMID: 17176066]

2. Shinoda, K., Hasegawa, T., Sato, H., Shinozaki, M., Kuramoto, H., Takamiya, Y., Sato, T., Nikaidou, N., Watanabe, T. and Hoshino, T. Biosynthesis of violacein: a genuine intermediate, protoviolaceinic acid, produced by VioABDE, and insight into VioC function. Chem. Commun. (Camb.) (2007) 4140-4142. [PMID: 17925955]

[EC 1.14.13.224 created 2016]

EC 1.14.13.225

Accepted name: F-actin monooxygenase

Reaction: [F-actin]-L-methionine + NADPH + O2 + H+ = [F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O

Other name(s): MICAL (gene name)

Systematic name: [F-actin]-L-methionine,NADPH:O2 S-oxidoreductase

Comments: The enzyme, characterized from the fruit fly Drosophila melanogaster, is a multi-domain oxidoreductase that acts as an F-actin disassembly factor. The enzyme selectively reduces two L-Met residues of F-actin, causing fragmentation of the filaments and preventing repolymerization [1]. Free methionine is not a substrate [2]. The reaction is stereospecific and generates the (R)-sulfoxide [3]. In the absence of substrate, the enzyme can act as an NAD(P)H oxidase (EC 1.6.3.1) [4,5].

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

References:

1. Hung, R.J., Yazdani, U., Yoon, J., Wu, H., Yang, T., Gupta, N., Huang, Z., van Berkel, W.J. and Terman, J.R. Mical links semaphorins to F-actin disassembly. Nature 463 (2010) 823-827. [PMID: 20148037]

2. Hung, R.J., Pak, C.W. and Terman, J.R. Direct redox regulation of F-actin assembly and disassembly by Mical. Science 334 (2011) 1710-1713. [PMID: 22116028]

3. Hung, R.J., Spaeth, C.S., Yesilyurt, H.G. and Terman, J.R. SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics. Nat. Cell Biol. 15 (2013) 1445-1454. [PMID: 24212093]

4. Zucchini, D., Caprini, G., Pasterkamp, R.J., Tedeschi, G. and Vanoni, M.A. Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1. Arch. Biochem. Biophys. 515 (2011) 1-13. [PMID: 21864500]

5. Vitali, T., Maffioli, E., Tedeschi, G. and Vanoni, M.A. Properties and catalytic activities of MICAL1, the flavoenzyme involved in cytoskeleton dynamics, and modulation by its CH, LIM and C-terminal domains. Arch. Biochem. Biophys. 593 (2016) 24-37. [PMID: 26845023]

[EC 1.14.13.225 created 2016]

EC 1.14.13.226

Accepted name: acetone monooxygenase (methylacetate-forming)

Reaction: acetone + NADPH + H+ + O2 = methylacetate + NADP+ + H2O

Other name(s): acmA (gene name)

Systematic name: acetone,NADPH:oxygen oxidoreductase (methylacetate-forming)

Comments: Contains FAD. The enzyme, characterized from the bacterium Gordonia sp. TY-5, is a Baeyer-Villiger type monooxygenase and participates in a propane utilization pathway.

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

References:

1. Kotani, T., Yurimoto, H., Kato, N. and Sakai, Y. Novel acetone metabolism in a propane-utilizing bacterium, Gordonia sp. strain TY-5. J. Bacteriol. 189 (2007) 886-893. [PMID: 17071761]

[EC 1.14.13.226 created 2016]

EC 1.14.13.227

Accepted name: propane 2-monooxygenase

Reaction: propane + NADH + H+ + O2 = propan-2-ol + NAD+ + H2O

Glossary: propan-2-ol = isopropanol

Other name(s): prmABCD (gene names)

Systematic name: propane,NADH:oxygen oxidoreductase (2-hydroxylating)

Comments: The enzyme, characterized from several bacterial strains, is a multicomponent dinuclear iron monooxygenase that includes a hydroxylase, an NADH-dependent reductase, and a coupling protein. The enzyme has several additional activities, including acetone monooxygenase (acetol-forming) and phenol 4-monooxygenase.

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

References:

1. Kotani, T., Yamamoto, T., Yurimoto, H., Sakai, Y. and Kato, N. Propane monooxygenase and NAD+-dependent secondary alcohol dehydrogenase in propane metabolism by Gordonia sp. strain TY-5. J. Bacteriol. 185 (2003) 7120-7128. [PMID: 14645271]

2. Sharp, J.O., Sales, C.M., LeBlanc, J.C., Liu, J., Wood, T.K., Eltis, L.D., Mohn, W.W. and Alvarez-Cohen, L. An inducible propane monooxygenase is responsible for N-nitrosodimethylamine degradation by Rhodococcus sp. strain RHA1. Appl. Environ. Microbiol. 73 (2007) 6930-6938. [PMID: 17873074]

3. Furuya, T., Hirose, S., Osanai, H., Semba, H. and Kino, K. Identification of the monooxygenase gene clusters responsible for the regioselective oxidation of phenol to hydroquinone in mycobacteria. Appl. Environ. Microbiol. 77 (2011) 1214-1220. [PMID: 21183637]

[EC 1.14.13.227 created 2016]

EC 1.14.13.228

Accepted name: jasmonic acid 12-hydroxylase

Reaction: (–)-jasmonate + NADPH + H+ + O2 = trans-12-hydroxyjasmonate + NADP+ + H2O

Glossary: (–)-jasmonate = {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetate
trans-12-hydroxyjasmonate = {(1R,2R)-2-[(2Z)-5-hydroxypent-2-en-1-yl]-3-oxocyclopentyl}acetate

Other name(s): ABM (gene name)

Systematic name: jasmonate,NADPH:oxygen oxidoreductase (12-hydroxylating)

Comments: Although believed to occur in plants, the enzyme has so far been characterized only from the rice blast fungus, Magnaporthe oryzae. The fungus strategically deploys the enzyme to hydroxylate and inactivate endogenous jasmonate to evade the jasmonate-based innate immunity in rice plants.

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

References:

1. Patkar, R.N., Benke, P.I., Qu, Z., Chen, Y.Y., Yang, F., Swarup, S. and Naqvi, N.I. A fungal monooxygenase-derived jasmonate attenuates host innate immunity. Nat. Chem. Biol. 11 (2015) 733-740. [PMID: 26258762]

[EC 1.14.13.228 created 2016]

EC 1.14.13.229

Accepted name: tert-butyl alcohol monooxygenase

Reaction: tert-butyl alcohol + NADPH + H+ + O2 = 2-methylpropane-1,2-diol + NADP+ + H2O

Other name(s): mdpJK (gene names); tert-butanol monooxygenase

Systematic name: tert-butyl alcohol,NADPH:oxygen oxidoreductase

Comments: The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, is a Rieske nonheme mononuclear iron oxygenase. It can also act, with lower efficiency, on propan-2-ol, converting it to propane-1,2-diol. Depending on the substrate, the enzyme also catalyses EC 1.14.19.48, tert-amyl alcohol desaturase.

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

References:

1. Schafer, F., Breuer, U., Benndorf, D., von Bergen, M., Harms, H. and Muller, R.H. Growth of Aquincola tertiaricarbonis L108 on tert-butyl alcohol leads to the induction of a phthalate dioxygenase-related protein and its associated oxidoreductase subunit. Eng. Life Sci. 7 (2007) 512-519.

2. Schuster, J., Schafer, F., Hubler, N., Brandt, A., Rosell, M., Hartig, C., Harms, H., Muller, R.H. and Rohwerder, T. Bacterial degradation of tert-amyl alcohol proceeds via hemiterpene 2-methyl-3-buten-2-ol by employing the tertiary alcohol desaturase function of the Rieske nonheme mononuclear iron oxygenase MdpJ. J. Bacteriol. 194 (2012) 972-981. [PMID: 22194447]

[EC 1.14.13.229 created 2016]

EC 1.14.13.230

Accepted name: butane monooxygenase (soluble)

Reaction: butane + NADH + H+ + O2 = butan-1-ol + NAD+ + H2O

Other name(s): sBMO; bmoBCDXYZ (gene names)

Systematic name: butane,NADH:oxygen oxidoreductase

Comments: The enzyme, characterized from the bacterium Thauera butanivorans, is similar to EC 1.14.13.25, methane monooxygenase (soluble), but has a very low activity with methane. It comprises three components - a carboxylate-bridged non-heme di-iron center-containing hydroxylase (made of three different subunits), a flavo-iron sulfur-containing NADH-oxidoreductase, and a small regulatory component protein. The enzyme can also act on other C3-C6 linear and branched aliphatic alkanes with lower activity.

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

References:

1. Sluis, M.K., Sayavedra-Soto, L.A. and Arp, D.J. Molecular analysis of the soluble butane monooxygenase from ‘Pseudomonas butanovora’. Microbiology 148 (2002) 3617-3629. [PMID: 12427952]

2. Dubbels, B.L., Sayavedra-Soto, L.A. and Arp, D.J. Butane monooxygenase of ‘Pseudomonas butanovora’: purification and biochemical characterization of a terminal-alkane hydroxylating diiron monooxygenase. Microbiology 153 (2007) 1808-1816. [PMID: 17526838]

3. Doughty, D.M., Kurth, E.G., Sayavedra-Soto, L.A., Arp, D.J. and Bottomley, P.J. Evidence for involvement of copper ions and redox state in regulation of butane monooxygenase in Pseudomonas butanovora. J. Bacteriol. 190 (2008) 2933-2938. [PMID: 18281403]

4. Cooley, R.B., Dubbels, B.L., Sayavedra-Soto, L.A., Bottomley, P.J. and Arp, D.J. Kinetic characterization of the soluble butane monooxygenase from Thauera butanivorans, formerly ‘Pseudomonas butanovora’. Microbiology 155 (2009) 2086-2096. [PMID: 19383682]

[EC 1.14.13.230 created 2016]

EC 1.14.13.231

Accepted name: tetracycline 11a-monooxygenase

Reaction: tetracycline + NADPH + H+ + O2 = 11a-hydroxytetracycline + NADP+ + H2O

For diagram of reaction click here.

Other name(s): tetX (gene name)

Systematic name: tetracycline,NADPH:oxygen oxidoreductase (11a-hydroxylating)

Comments: A flavoprotein (FAD). This bacterial enzyme confers resistance to all clinically relevant tetracyclines when expressed under aerobic conditions. The hydroxylated products are very unstable and lead to intramolecular cyclization and non-enzymic breakdown to undefined products.

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

References:

1. Yang, W., Moore, I.F., Koteva, K.P., Bareich, D.C., Hughes, D.W. and Wright, G.D. TetX is a flavin-dependent monooxygenase conferring resistance to tetracycline antibiotics. J. Biol. Chem. 279 (2004) 52346-52352. [PMID: 15452119]

2. Moore, I.F., Hughes, D.W. and Wright, G.D. Tigecycline is modified by the flavin-dependent monooxygenase TetX. Biochemistry 44 (2005) 11829-11835. [PMID: 16128584]

3. Volkers, G., Palm, G.J., Weiss, M.S., Wright, G.D. and Hinrichs, W. Structural basis for a new tetracycline resistance mechanism relying on the TetX monooxygenase. FEBS Lett. 585 (2011) 1061-1066. [PMID: 21402075]

[EC 1.14.13.231 created 2016]

EC 1.14.13.232

Accepted name: 6-methylpretetramide 4-monooxygenase

Reaction: 6-methylpretetramide + NADPH + H+ + O2 = 4-hydroxy-6-methylpretetramide + NADP+ + H2O

For diagram of reaction click here.

Glossary: 6-methylpretetramide = 1,3,10,11,12-pentahydroxy-6-methyltetracene-2-carboxamide
4-hydroxy-6-methylpretetramide = 1,3,4,10,11,12-hexahydroxy-6-methyltetracene-2-carboxamide

Systematic name: 6-methylpretetramide,NADPH:oxygen oxidoreductase (4-hydroxylating)

Comments: The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. That bacterium possesses two enzymes that can catalyse the reaction - OxyE is the main isozyme, while OxyL has a lower activity. OxyL is bifunctional, and its main function is EC 1.14.13.233, 4-hydroxy-6-methylpretetramide 12a-monooxygenase. Contains FAD.

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

References:

1. Zhang, W., Watanabe, K., Cai, X., Jung, M.E., Tang, Y. and Zhan, J. Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. J. Am. Chem. Soc. 130 (2008) 6068-6069. [PMID: 18422316]

2. Wang, P., Zhang, W., Zhan, J. and Tang, Y. Identification of OxyE as an ancillary oxygenase during tetracycline biosynthesis. Chembiochem 10 (2009) 1544-1550. [PMID: 19472250]

[EC 1.14.13.232 created 2016]

EC 1.14.13.233

Accepted name: 4-hydroxy-6-methylpretetramide 12a-monooxygenase

Reaction: 4-hydroxy-6-methylpretetramide + NADPH + H+ + O2 = 4-de(dimethylamino)-4-oxoanhydrotetracycline + NADP+ + H2O

For diagram of reaction click here.

Glossary: 4-hydroxy-6-methylpretetramide = 1,3,4,10,11,12-hexahydroxy-6-methyltetracene-2-carboxamide
4-de(dimethylamino)-4-oxoanhydrotetracycline = (4aR,12aS)-3,10,11,12a-tetrahydroxy-6-methyl-1,4,12-trioxo-4a,5-dihydrotetracene-2-carboxamide

Other name(s): oxyL (gene name)

Systematic name: 4-hydroxy-6-methylpretetramide,NADPH:oxygen oxidoreductase (12a-hydroxylating)

Comments: Contains FAD. The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. The enzyme is bifunctional, and can also catalyse EC 1.14.13.232, 6-methylpretetramide 4-monooxygenase.

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

References:

1. Zhang, W., Watanabe, K., Cai, X., Jung, M.E., Tang, Y. and Zhan, J. Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. J. Am. Chem. Soc. 130 (2008) 6068-6069. [PMID: 18422316]

[EC 1.14.13.233 created 2016]

EC 1.14.13.234

Accepted name: 5a,11a-dehydrotetracycline 5-monooxygenase

Reaction: 5a,11a-dehydrotetracycline + NADPH + H+ + O2 = 5a,11a-dehydrooxytetracycline + NADP+ + H2O

For diagram of reaction click here.

Glossary: 5a,11a-dehydrotetracycline = 12-dehydrotetracycline = (4S,4aS,6S,12aS)-4-dimethylamino-3,6,10,12a-tetrahydroxy-6-methyl-1,11,12-trioxo-1,4,4a,5,6,11,12,12a-octahydrotetracene-2-carboxamide

Other name(s): oxyS (gene name); 12-dehydrotetracycline 5-monooxygenase

Systematic name: 5a,11a-dehydrotetracycline,NADPH:oxygen oxidoreductase (5-hydroxylating)

Comments: The enzyme, characterized from the bacterium Streptomyces rimosus, is bifunctional, catalysing two successive monooxygenation reactions. It starts by catalysing the stereospecific hydroxylation of anhydrotetracycline at C-6 (EC 1.14.13.38). If the released product is captured by EC 1.3.98.4, 5a,11a-dehydrotetracycline dehydrogenase (OxyR), it is reduced to tetracycline. However, if the released product is recaptured by OxyS, it performs an additional hydroxylation at C-5, producing 5a,11a-dehydrooxytetracycline, which, following the action of OxyR, becomes oxytetracycline.

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

References:

1. Binnie, C., Warren, M. and Butler, M.J. Cloning and heterologous expression in Streptomyces lividans of Streptomyces rimosus genes involved in oxytetracycline biosynthesis. J. Bacteriol. 171 (1989) 887-895. [PMID: 2914874]

2. Miller, P.A., Saturnelli, A., Martin, J.H., Itscher, L.A. and Bohonos, N. A new family of tetracycline precursors. N-demethylanhydrotetracyclines. Biochem. Biophys. Res. Commun. 16 (1964) 285-291. [PMID: 4959040]

3. Vancurova, I., Volc, J., Flieger, M., Neuzil, J., Novotna, J., Vlach, J. and Behal, V. Isolation of pure anhydrotetracycline oxygenase from Streptomyces aureofaciens. Biochem. J. 253 (1988) 263-267. [PMID: 3138982]

4. Wang, P., Bashiri, G., Gao, X., Sawaya, M.R. and Tang, Y. Uncovering the enzymes that catalyze the final steps in oxytetracycline biosynthesis. J. Am. Chem. Soc. 135 (2013) 7138-7141. [PMID: 23621493]

[EC 1.14.13.234 created 2016]

EC 1.14.13.235

Accepted name: indole-3-acetate monooxygenase

Reaction: (indol-3-yl)acetate + NADH + H+ + O2 = (2-hydroxy-1H-indol-3-yl)acetate + NAD+ + H2O

Glossary: (indol-3-yl)acetate =(1H-indol-3-yl)acetate = indole-3-acetate

Other name(s): iacA (gene name)

Systematic name: (indol-3-yl)acetate,NADH:oxygen oxidoreductase (2-hydroxylating)

Comments: The enzyme, characterized from Pseudomonas putida strains, catalyses the first step in a pathway for degradation of the plant hormone indole-3-acetate. When acting on indole, the enzyme forms indoxyl, which reacts spontaneously with oxygen to form the blue dye indigo.

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

References:

1. Leveau, J.H. and Lindow, S.E. Utilization of the plant hormone indole-3-acetic acid for growth by Pseudomonas putida strain 1290. Appl. Environ. Microbiol. 71 (2005) 2365-2371. [PMID: 15870323]

2. Scott, J.C., Greenhut, I.V. and Leveau, J.H. Functional characterization of the bacterial iac genes for degradation of the plant hormone indole-3-acetic acid. J Chem Ecol 39 (2013) 942-951. [PMID: 23881445]

[EC 1.14.13.235 created 2017]

EC 1.14.13.236

Accepted name: toluene 4-monooxygenase

Reaction: toluene + NADH + H+ + O2 = 4-methylphenol + NAD+ + H2O

Glossary: 4-methylphenol = p-cresol

Other name(s): TMO

Systematic name: toluene,NADH:oxygen oxidoreductase (4-hydroxylating)

Comments: This bacterial enzyme belongs to a family of soluble diiron hydroxylases that includes toluene-, benzene-, xylene- and methane monooxygenases, phenol hydroxylases, and alkene epoxidases. The enzyme comprises a four-component complex that includes a hydroxylase, NADH-ferredoxin oxidoreductase, a Rieske-type [2Fe-2S] ferredoxin, and an effector protein.

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

References:

1. Whited, G.M. and Gibson, D.T. Toluene-4-monooxygenase, a three-component enzyme system that catalyzes the oxidation of toluene to p-cresol in Pseudomonas mendocina KR1. J. Bacteriol. 173 (1991) 3010-3016. [PMID: 2019563]

2. Hemmi, H., Studts, J.M., Chae, Y.K., Song, J., Markley, J.L. and Fox, B.G. Solution structure of the toluene 4-monooxygenase effector protein (T4moD). Biochemistry 40 (2001) 3512-3524. [PMID: 11297417]

3. Schwartz, J.K., Wei, P.P., Mitchell, K.H., Fox, B.G. and Solomon, E.I. Geometric and electronic structure studies of the binuclear nonheme ferrous active site of toluene-4-monooxygenase: parallels with methane monooxygenase and insight into the role of the effector proteins in O2 activation. J. Am. Chem. Soc. 130 (2008) 7098-7109. [PMID: 18479085]

4. Bailey, L.J., Acheson, J.F., McCoy, J.G., Elsen, N.L., Phillips, G.N., Jr. and Fox, B.G. Crystallographic analysis of active site contributions to regiospecificity in the diiron enzyme toluene 4-monooxygenase. Biochemistry 51 (2012) 1101-1113. [PMID: 22264099]

5. Hosseini, A., Brouk, M., Lucas, M.F., Glaser, F., Fishman, A. and Guallar, V. Atomic picture of ligand migration in toluene 4-monooxygenase. J. Phys. Chem. B 119 (2015) 671-678. [PMID: 24798294]

[EC 1.14.13.236 created 2017]

EC 1.14.13.237

Accepted name: aliphatic glucosinolate S-oxygenase

Reaction: an ω-(methylsulfanyl)alkyl-glucosinolate + NADPH + H+ + O2 = an ω-(methylsulfinyl)alkyl-glucosinolate + NADP+ + H2O

Glossary: ω-(methylsulfanyl)alkyl-glucosinolate = an ω-(methylsulfanyl)-N-sulfo-alkylhydroximate S-glucoside

Other name(s): ω-(methylthio)alkylglucosinolate S-oxygenase; GS-OX1 (gene name)

Systematic name: ω-(methylsulfanyl)alkyl-glucosinolate,NADPH:oxygen S-oxidoreductase

Comments: The enzyme is a member of the flavin-dependent monooxygenase (FMO) family (cf. EC 1.14.13.8). The plant Arabidopsis thaliana contains five isoforms. GS-OX1 through GS-OX4 are able to catalyse the S-oxygenation independent of chain length, while GS-OX5 is specific for 8-(methylthio)octyl glucosinolate.

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

References:

1. Hansen, B.G., Kliebenstein, D.J. and Halkier, B.A. Identification of a flavin-monooxygenase as the S-oxygenating enzyme in aliphatic glucosinolate biosynthesis in Arabidopsis. Plant J. 50 (2007) 902-910. [PMID: 17461789]

2. Li, J., Hansen, B.G., Ober, J.A., Kliebenstein, D.J. and Halkier, B.A. Subclade of flavin-monooxygenases involved in aliphatic glucosinolate biosynthesis. Plant Physiol. 148 (2008) 1721-1733. [PMID: 18799661]

[EC 1.14.13.237 created 2017]

EC 1.14.13.238

Accepted name: dimethylamine monooxygenase

Reaction: dimethylamine + NADPH + H+ + O2 = methylamine + formaldehyde + NADP+ + H2O

Other name(s): dmmABC (gene names)

Systematic name: dimethylamine,NADPH:oxygen oxidoreductase (formaldehyde-forming)

Comments: The enzyme, characterized from several bacterial species, is involved in a pathway for the degradation of methylated amines. It is composed of three subunits, one of which is a ferredoxin, and contains heme iron and an FMN cofactor.

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

References:

1. Eady, R.R. and Large, P.J. Bacterial oxidation of dimethylamine, a new mono-oxygenase reaction. Biochem. J. 111 (1969) 37P-38P. [PMID: 4389011]

2. Eady, R.R., Jarman, T.R. and Large, P.J. Microbial oxidation of amines. Partial purification of a mixed-function secondary-amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome-P-420-type haemoprotein. Biochem. J. 125 (1971) 449-459. [PMID: 4401380]

3. Alberta, J.A. and Dawson, J.H. Purification to homogeneity and initial physical characterization of secondary amine monooxygenase. J. Biol. Chem. 262 (1987) 11857-11863. [PMID: 3624236]

4. Lidbury, I., Mausz, M.A., Scanlan, D.J. and Chen, Y. Identification of dimethylamine monooxygenase in marine bacteria reveals a metabolic bottleneck in the methylated amine degradation pathway. LID - 10.1038/ismej.2017.31 [doi. ISME J. (2017) . [PMID: 28304370]

[EC 1.14.13.238 created 2017]

EC 1.14.13.239

Accepted name: carnitine monooxygenase

Reaction: L-carnitine + NAD(P)H + H+ + O2 = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD(P)+ + H2O

Glossary: (3R)-3-hydroxy-4-oxobutanoate = L-malic semialdehyde

Other name(s): cntAB (gene names); yeaWX (gene names)

Systematic name: L-carnitine,NAD(P)H:oxygen oxidoreductase (trimethylamine-forming)

Comments: The bacterial enzyme is a complex consisting of a reductase and an oxygenase components. The reductase subunit contains a flavin and a plant-type ferredoxin [2Fe-2S] cluster, while the oxygenase subunit is a Rieske-type protein in which a [2Fe-2S] cluster is coordinated by two histidine and two cysteine residues.

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

References:

1. Ditullio, D., Anderson, D., Chen, C.S. and Sih, C.J. L-carnitine via enzyme-catalyzed oxidative kinetic resolution. Bioorg. Med. Chem. 2 (1994) 415-420. [PMID: 8000862]

2. Zhu, Y., Jameson, E., Crosatti, M., Schafer, H., Rajakumar, K., Bugg, T.D. and Chen, Y. Carnitine metabolism to trimethylamine by an unusual Rieske-type oxygenase from human microbiota. Proc. Natl Acad. Sci. USA 111 (2014) 4268-4273. [PMID: 24591617]

3. Koeth, R.A., Levison, B.S., Culley, M.K., Buffa, J.A., Wang, Z., Gregory, J.C., Org, E., Wu, Y., Li, L., Smith, J.D., Tang, W.H., DiDonato, J.A., Lusis, A.J. and Hazen, S.L. γ-Butyrobetaine is a proatherogenic intermediate in gut microbial metabolism of L-carnitine to TMAO. Cell Metab 20 (2014) 799-812. [PMID: 25440057]

[EC 1.14.13.239 created 2017]

EC 1.14.13.240

Accepted name: 2-polyprenylphenol 6-hydroxylase

Reaction: 2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2 = 3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O

For diagram of reaction click here.

Other name(s): ubiI (gene name); ubiM (gene name)

Systematic name: 2-(all-trans-polyprenyl)phenol,NADPH:oxygen oxidoreductase (6-hydroxylating)

Comments: Contains FAD. The enzyme from the bacterium Escherichia coli (UbiI) catalyses the first hydroxylation during the aerobic biosynthesis of ubiquinone. The enzyme from the bacterium Neisseria meningitidis (UbiM) can also catalyse the two additional hydroxylations that occur in the pathway (cf. EC 1.14.99.60, 3-demethoxyubiquinol 3-hydroxylase).

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

References:

1. Hajj Chehade, M., Loiseau, L., Lombard, M., Pecqueur, L., Ismail, A., Smadja, M., Golinelli-Pimpaneau, B., Mellot-Draznieks, C., Hamelin, O., Aussel, L., Kieffer-Jaquinod, S., Labessan, N., Barras, F., Fontecave, M. and Pierrel, F. ubiI, a new gene in Escherichia coli coenzyme Q biosynthesis, is involved in aerobic C5-hydroxylation. J. Biol. Chem 288 (2013) 20085–20092. [PMID: 23709220]

2. Pelosi, L., Ducluzeau, A.L., Loiseau, L., Barras, F., Schneider, D., Junier, I. and Pierrel, F. Evolution of Ubiquinone Biosynthesis: Multiple Proteobacterial Enzymes with Various Regioselectivities To Catalyze Three Contiguous Aromatic Hydroxylation Reactions. mSystems 1 (2016) . [PMID: 27822549]

[EC 1.14.13.240 created 2018]

EC 1.14.13.241

Accepted name: 5-pyridoxate monooxygenase

Reaction: 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + H+ + O2 = 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+

Glossary: 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate = 5-pyridoxate

Other name(s): 5-pyridoxate,NADPH:oxygen oxidoreductase (decyclizing); 5-pyridoxate oxidase (misleading); 5-pyridoxate dioxygenase (incorrect)

Systematic name: 5-pyridoxate,NADPH:oxygen oxidoreductase (ring-opening)

Comments: Contains FAD. The enzyme, characterized from the bacterium Arthrobacter sp. Cr-7, participates in the degradation of pyridoxine (vitamin B6). Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have suggested that it is a monooxygenase, incorporating only one oxygen atom from molecular oxygen into the product. The second oxygen atom originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.

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

References:

1. Sparrow, L.G., Ho, P.P.K., Sundaram, T.K., Zach, D., Nyns, E.J. and Snell, E.E. The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3-hydroxypyridine ring. J. Biol. Chem. 244 (1969) 2590-2600. [PMID: 4306031]

2. Nelson, M.J. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of 5-pyridoxic-acid oxygenase from Arthrobacter sp. J. Biol. Chem 261 (1986) 15115-15120. [PMID: 3771566]

3. Chaiyen, P. Flavoenzymes catalyzing oxidative aromatic ring-cleavage reactions. Arch. Biochem. Biophys. 493 (2010) 62-70. [PMID: 19728986]

[EC 1.14.13.241 created 2018 (EC 1.14.12.5 created 1972, incorporated 2018)]

EC 1.14.13.242

Accepted name: 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase

Reaction: 3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+

For diagram of reaction click here.

Other name(s): MHPCO; 3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (decyclizing); methylhydroxypyridinecarboxylate oxidase (misleading); 2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase (incorrect); methylhydroxypyridine carboxylate dioxygenase (incorrect); 3-hydroxy-3-methylpyridinecarboxylate dioxygenase [incorrect]; 3-hydroxy-2-methylpyridinecarboxylate dioxygenase (incorrect)

Systematic name: 3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (ring-opening)

Comments: Contains FAD. The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6). Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have shown that it is a monooxygenase, incorporating only one oxygen atom from molecular oxygen. The second oxygen atom that is incorporated into the product originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.

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

References:

1. Sparrow, L.G., Ho, P.P.K., Sundaram, T.K., Zach, D., Nyns, E.J. and Snell, E.E. The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3-hydroxypyridine ring. J. Biol. Chem. 244 (1969) 2590-2600. [PMID: 4306031]

2. Chaiyen, P., Ballou, D.P. and Massey, V. Gene cloning, sequence analysis, and expression of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase. Proc. Natl Acad. Sci. USA 94 (1997) 7233-7238. [PMID: 9207074]

3. Oonanant, W., Sucharitakul, J., Yuvaniyama, J. and Chaiyen, P. Crystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 312-314. [PMID: 16511028]

4. Yuan, B., Yokochi, N., Yoshikane, Y., Ohnishi, K. and Yagi, T. Molecular cloning, identification and characterization of 2-methyl-3-hydroxypyridine-5-carboxylic-acid-dioxygenase-coding gene from the nitrogen-fixing symbiotic bacterium Mesorhizobium loti. J. Biosci. Bioeng. 102 (2006) 504-510. [PMID: 17270714]

5. McCulloch, K.M., Mukherjee, T., Begley, T.P. and Ealick, S.E. Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications. Biochemistry 48 (2009) 4139-4149. [PMID: 19317437]

6. Tian, B., Tu, Y., Strid, A. and Eriksson, L.A. Hydroxylation and ring-opening mechanism of an unusual flavoprotein monooxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: a theoretical study. Chemistry 16 (2010) 2557-2566. [PMID: 20066695]

7. Tian, B., Strid, A. and Eriksson, L.A. Catalytic roles of active-site residues in 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: an ONIOM/DFT study. J. Phys. Chem. B 115 (2011) 1918-1926. [PMID: 21291225]

[EC 1.14.13.242 created 2018 (EC 1.14.12.4 created 1972, incorporated 2018)]

EC 1.14.13.243

Accepted name: toluene 2-monooxygenase

Reaction: (1) toluene + NADH + H+ + O2 = 2-methylphenol + NAD+ + H2O
(2) 2-methylphenol + NADH + H+ + O2 = 3-methylcatechol + NAD+ + H2O

Other name(s): tomA1/2/3/4/5 (gene names); toluene ortho-monooxygenase

Systematic name: toluene,NADH:oxygen oxidoreductase (2,3-dihydroxylating)

Comments: The enzyme, characterized from the bacterium Burkholderia cepacia, belongs to a class of nonheme, oxygen-dependent diiron enzymes. It contains a hydroxylase component with two binuclear iron centers, an NADH-oxidoreductase component containing FAD and a [2Fe-2S] iron-sulfur cluster, and a third component involved in electron transfer between the hydroxylase and the reductase. The enzyme dihydroxylates its substrate in two sequential hydroxylations, initially forming 2-methylphenol, which is hydroxylated to 3-methylcatechol.

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

References:

1. Newman, L.M. and Wackett, L.P. Purification and characterization of toluene 2-monooxygenase from Burkholderia cepacia G4. Biochemistry 34 (1995) 14066-14076. [PMID: 7578004]

2. Yeager, C.M., Bottomley, P.J., Arp, D.J. and Hyman, M.R. Inactivation of toluene 2-monooxygenase in Burkholderia cepacia G4 by alkynes. Appl. Environ. Microbiol. 65 (1999) 632-639. [PMID: 9925593]

3. Canada, K.A., Iwashita, S., Shim, H. and Wood, T.K. Directed evolution of toluene ortho-monooxygenase for enhanced 1-naphthol synthesis and chlorinated ethene degradation. J. Bacteriol. 184 (2002) 344-349. [PMID: 11751810]

[EC 1.14.13.243 created 2019]

EC 1.14.13.244

Accepted name: phenol 2-monooxygenase (NADH)

Reaction: phenol + NADH + H+ + O2 = catechol + NAD+ + H2O

For diagram of reaction click here.

Other name(s): dmpLMNOP (gene names)

Systematic name: phenol,NADH:oxygen oxidoreductase (2-hydroxylating)

Comments: The enzyme, characterized from the bacteria Pseudomonas sp. CF600 and Acinetobacter radioresistens, consists of a multisubunit oxygenease component that contains the active site and a dinuclear iron center, a reductase component that contains FAD and one iron-sulfur cluster, and a regulatory component. The reductase component is responsible for transferring electrons from NADH to the dinuclear iron center.

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

References:

1. Nordlund, I., Powlowski, J. and Shingler, V. Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Bacteriol. 172 (1990) 6826-6833. [PMID: 2254258]

2. Powlowski, J. and Shingler, V. In vitro analysis of polypeptide requirements of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Bacteriol. 172 (1990) 6834-6840. [PMID: 2254259]

3. Powlowski, J., Sealy, J., Shingler, V. and Cadieux, E. On the role of DmpK, an auxiliary protein associated with multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Biol. Chem 272 (1997) 945-951. [PMID: 8995386]

4. Qian, H., Edlund, U., Powlowski, J., Shingler, V. and Sethson, I. Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy. Biochemistry 36 (1997) 495-504. [PMID: 9012665]

5. Cadieux, E., Vrajmasu, V., Achim, C., Powlowski, J. and Munck, E. Biochemical, Mossbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600. Biochemistry 41 (2002) 10680-10691. [PMID: 12186554]

[EC 1.14.13.244 created 2019]

EC 1.14.13.245

Accepted name: assimilatory dimethylsulfide S-monooxygenase

Reaction: (1) dimethyl sulfide + NADH + H+ + O2 = dimethyl sulfoxide + NAD+ + H2O
(2) dimethyl sulfoxide + NADH + H+ + O2 = dimethyl sulfone + NAD+ + H2O

For diagram of reaction click here.

Other name(s): dsoBCDEF (gene names)

Systematic name: dimethyl sulfide,NADH:oxygen oxidoreductase (S-oxidizing)

Comments: The enzyme, studied from the bacterium Acinetobacter sp. strain 20B, is very similar to EC 1.14.13.244, phenol 2-monooxygenase (NADH). It consists of a multisubunit oxygenease component that contains the active site and a dinuclear iron center, a reductase component that contains FAD and one iron-sulfur cluster, and a regulatory component. The three components comprise five different polypeptides. The enzyme catalyses the first two steps of a dimethyl sulfide oxidation pathway in this organism.

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

References:

1. Horinouchi, M., Kasuga, K., Nojiri, H., Yamane, H. and Omori, T. Cloning and characterization of genes encoding an enzyme which oxidizes dimethyl sulfide in Acinetobacter sp. strain 20B. FEMS Microbiol. Lett. 155 (1997) 99-105. [PMID: 9345770]

2. Horinouchi, M., Yoshida, T., Nojiri, H., Yamane, H. and Omori, T. Polypeptide requirement of multicomponent monooxygenase DsoABCDEF for dimethyl sulfide oxidizing activity. Biosci. Biotechnol. Biochem. 63 (1999) 1765-1771. [PMID: 26300166]

[EC 1.14.13.245 created 2019]


Continued with EC 1.14.14
Return to EC 1 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page