ExplorEnz: EC 1.14.13.2*

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1.14.13.2

Accepted name:

4-hydroxybenzoate 3-monooxygenase

Reaction:

4-hydroxybenzoate + NADPH + H⁺ + O₂ = 3,4-dihydroxybenzoate + NADP⁺ + H₂O

For diagram of benzoate metabolism, click here

Glossary:

3,4-dihydroxybenzoate = protocatechuate

Other name(s):

p-hydroxybenzoate hydrolyase; p-hydroxybenzoate hydroxylase; 4-hydroxybenzoate 3-hydroxylase; 4-hydroxybenzoate monooxygenase; 4-hydroxybenzoic hydroxylase; p-hydroxybenzoate-3-hydroxylase; p-hydroxybenzoic acid hydrolase; p-hydroxybenzoic acid hydroxylase; p-hydroxybenzoic hydroxylase

Systematic name:

4-hydroxybenzoate,NADPH:oxygen oxidoreductase (3-hydroxylating)

Comments:

A flavoprotein (FAD). Most enzymes from Pseudomonas are highly specific for NADPH (cf. EC 1.14.13.33 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]).

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9059-23-8

References:

1.	Hosokawa, K. and Stanier, R.Y. Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida. J. Biol. Chem. 241 (1966) 2453–2460. [PMID: 4380381]
2.	Howell, L.G., Spector, T. and Massey, V. Purification and properties of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. J. Biol. Chem. 247 (1972) 4340–4350. [PMID: 4402514]
3.	Spector, T. and Massey, V. Studies on the effector specificity of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. J. Biol. Chem. 247 (1972) 4679–4687. [PMID: 4402938]
4.	Spector, T. and Massey, V. p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Evidence for an oxygenated flavin intermediate. J. Biol. Chem. 247 (1972) 5632–5636. [PMID: 4403446]
5.	Spector, T. and Massey, V. p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Reactivity with oxygen. J. Biol. Chem. 247 (1972) 7123–7127. [PMID: 4404745]
6.	Seibold, B., Matthes, M., Eppink, M.H., Lingens, F., Van Berkel, W.J. and Muller, R. 4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3. Purification, characterization, gene cloning, sequence analysis and assignment of structural features determining the coenzyme specificity. Eur. J. Biochem. 239 (1996) 469–478. [DOI] [PMID: 8706756]

[EC 1.14.13.2 created 1972, modified 1999]

1.14.13.20

Accepted name:

2,4-dichlorophenol 6-monooxygenase

Reaction:

2,4-dichlorophenol + NADPH + H⁺ + O₂ = 3,5-dichlorocatechol + NADP⁺ + H₂O

Other name(s):

2,4-dichlorophenol hydroxylase; 2,4-dichlorophenol monooxygenase

Systematic name:

2,4-dichlorophenol,NADPH:oxygen oxidoreductase (6-hydroxylating)

Comments:

A flavoprotein (FAD). Also acts, more slowly, on 4-chlorophenol and 4-chloro-2-methylphenol; NADH can act instead of NADPH, but more slowly.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 82047-82-3

References:

1.	Beadle, C.A. and Smith, A.R.W. The purification and properties of 2,4-dichlorophenol hydroxylase from a strain of Acinetobacter species. Eur. J. Biochem. 123 (1982) 323–332. [DOI] [PMID: 7075592]

[EC 1.14.13.20 created 1983]

1.14.13.21

Transferred entry:

flavonoid 3′-monooxygenase. Now EC 1.14.14.82, flavonoid 3′-monooxygenase.

[EC 1.14.13.21 created 1983, deleted 2018]

1.14.13.22

Accepted name:

cyclohexanone monooxygenase

Reaction:

cyclohexanone + NADPH + H⁺ + O₂ = hexano-6-lactone + NADP⁺ + H₂O

For diagram of reaction, click here

Other name(s):

cyclohexanone 1,2-monooxygenase; cyclohexanone oxygenase; cyclohexanone:NADPH:oxygen oxidoreductase (6-hydroxylating, 1,2-lactonizing)

Systematic name:

cyclohexanone,NADPH:oxygen oxidoreductase (lactone-forming)

Comments:

A flavoprotein (FAD). In the catalytic mechanism of this enzyme, the nucleophilic species that attacks the carbonyl group is a peroxyflavin intermediate that is generated by reaction of the enzyme-bound flavin cofactor with NAD(P)H and oxygen [2]. This enzyme is able to catalyse a wide range of oxidative reactions, including enantioselective Baeyer-Villiger reactions [3], sulfoxidations [4], amine oxidations [5] and epoxidations [6].

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52037-90-8

References:

1.	Donoghue, N.A., Morris, D.B. and Trudgill, P.W. The purification and properties of cyclohexanone oxygenase from Nocardia globerula CL1 and Acinetobacter NCIB 9871. Eur. J. Biochem. 63 (1976) 175–192. [DOI] [PMID: 1261545]
2.	Sheng, D., Ballou, D.P. and Massey, V. Mechanistic studies of cyclohexanone monooxygenase: chemical properties of intermediates involved in catalysis. Biochemistry 40 (2001) 11156–11167. [DOI] [PMID: 11551214]
3.	Stewart, J.D. Cyclohexanone monooxygenase: a useful reagent for asymmetric Baeyer-Villiger reactions. Curr. Org. Chem. 2 (1998) 195–216.
4.	Chen, G., Kayser, M.M., Milhovilovic, M.D., Mrstik, M.E., Martinez, C.A. and Stewart, J.D. Asymmetric oxidations at sulfur catalyzed by engineered strains that overexpress cyclohexanone monooxygenase. New J. Chem. 23 (1999) 827–832.
5.	Ottolina, G., Bianchi, S., Belloni, B., Carrea, G. and Danieli, B. First asymmetric oxidation of tertiary amines by cyclohexanone monooxygenase. Tetrahedron Lett. 40 (1999) 8483–8486.
6.	Colonna, S., Gaggero, N., Carrea, G., Ottolina, G., Pasta, P. and Zambianchi, F. First asymmetric epoxidation catalysed by cyclohexanone monooxygenase. Tetrahedron Lett. 43 (2002) 1797–1799.

[EC 1.14.13.22 created 1984, modified 2004]

1.14.13.23

Accepted name:

3-hydroxybenzoate 4-monooxygenase

Reaction:

3-hydroxybenzoate + NADPH + H⁺ + O₂ = 3,4-dihydroxybenzoate + NADP⁺ + H₂O

Other name(s):

3-hydroxybenzoate 4-hydroxylase

Systematic name:

3-hydroxybenzoate,NADPH:oxygen oxidoreductase (4-hydroxylating)

Comments:

A flavoprotein (FAD). Acts also on a number of analogues of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-76-1

References:

1.	Michalover, J.L. and Ribbons, D.W. 3-Hydroxybenzoate 4-hydroxylase from Pseudomonas testosteroni. Biochem. Biophys. Res. Commun. 55 (1973) 888–896. [DOI] [PMID: 4148586]
2.	Premkumar, R., Subba Rao, P.V., Streeleela, N.S. and Vaidyanathan, C.S. m-Hydroxybenzoic acid 4-hydroxylase from Aspergillus niger. Can. J. Biochem. 47 (1969) 825–827. [PMID: 4390252]

[EC 1.14.13.23 created 1972 as EC 1.14.99.13, transferred 1984 to EC 1.14.13.23]

1.14.13.24

Accepted name:

3-hydroxybenzoate 6-monooxygenase

Reaction:

3-hydroxybenzoate + NADH + H⁺ + O₂ = 2,5-dihydroxybenzoate + NAD⁺ + H₂O

Other name(s):

3-hydroxybenzoate 6-hydroxylase; m-hydroxybenzoate 6-hydroxylase; 3-hydroxybenzoic acid-6-hydroxylase

Systematic name:

3-hydroxybenzoate,NADH:oxygen oxidoreductase (6-hydroxylating)

Comments:

A flavoprotein (FAD). Acts also on a number of analogues of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions; NADPH can act instead of NADH, but more slowly.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 51570-26-4

References:

1.	Groseclose, E.E. and Ribbons, D.W. 3-Hydroxybenzoate 6-hydroxylase from Pseudomonas aeruginosa. Biochem. Biophys. Res. Commun. 55 (1973) 897–903. [DOI] [PMID: 4357436]

[EC 1.14.13.24 created 1984]

1.14.13.25

Accepted name:

methane monooxygenase (soluble)

Reaction:

methane + NAD(P)H + H⁺ + O₂ = methanol + NAD(P)⁺ + H₂O

Other name(s):

methane hydroxylase

Systematic name:

methane,NAD(P)H:oxygen oxidoreductase (hydroxylating)

Comments:

The enzyme is soluble, in contrast to the particulate enzyme, EC 1.14.18.3. Broad specificity; many alkanes can be hydroxylated, and alkenes are converted into the corresponding epoxides; CO is oxidized to CO₂, ammonia is oxidized to hydroxylamine, and some aromatic compounds and cyclic alkanes can also be hydroxylated, but more slowly.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 51961-97-8

References:

1.	Colby, J. Stirling, D.I. and Dalton, H. The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds. Biochem. J. 165 (1977) 395–402. [PMID: 411486]
2.	Hyman, M.R. and Wood, P.M. Methane oxidation by Nitrosomonas europaea. Biochem. J. 212 (1983) 31–37. [PMID: 6870854]
3.	Stirling, D.I. and Dalton, H. Properties of the methane mono-oxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath). Eur. J. Biochem. 96 (1979) 205–212. [DOI] [PMID: 572296]
4.	Tonge, G.M., Harrison, D.E.F. and Higgins, I.J. Purification and properties of the methane mono-oxygenase enzyme system from Methylosinus trichosporium OB3b. Biochem. J. 161 (1977) 333–344. [PMID: 15544]

[EC 1.14.13.25 created 1984, modified 2011]

1.14.13.26

Transferred entry:

phosphatidylcholine 12-monooxygenase. Now classified as EC 1.14.18.4, phosphatidylcholine 12-monooxygenase.

[EC 1.14.13.26 created 1984, deleted 2015]

1.14.13.27

Accepted name:

4-aminobenzoate 1-monooxygenase

Reaction:

4-aminobenzoate + NAD(P)H + 2 H⁺ + O₂ = 4-hydroxyaniline + NAD(P)⁺ + H₂O + CO₂

Other name(s):

4-aminobenzoate hydroxylase; 4-aminobenzoate monooxygenase

Systematic name:

4-aminobenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating, decarboxylating)

Comments:

A flavoprotein (FAD). Acts on anthranilate and 4-aminosalicylate but not on salicylate (cf. EC 1.14.13.1 salicylate 1-monooxygenase).

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 98668-55-4

References:

1.	Tsuji, H., Ogawa, T., Bando, N. and Sasaoka, K. Purification and properties of 4-aminobenzoate hydroxylase, a new monooxygenase from Agaricus bisporus. J. Biol. Chem. 261 (1986) 13203–13209. [PMID: 3489713]

[EC 1.14.13.27 created 1989]

1.14.13.28

Transferred entry:

3,9-dihydroxypterocarpan 6a-monooxygenase. Now EC 1.14.14.93, 3,9-dihydroxypterocarpan 6a-monooxygenase

[EC 1.14.13.28 created 1989, deleted 2018]

1.14.13.29

Accepted name:

4-nitrophenol 2-monooxygenase

Reaction:

4-nitrophenol + NADH + H⁺ + O₂ = 4-nitrocatechol + NAD⁺ + H₂O

For diagram of 4-nitrophenol metabolism, click here

Other name(s):

4-nitrophenol hydroxylase; 4-nitrophenol-2-hydroxylase

Systematic name:

4-nitrophenol,NADH:oxygen oxidoreductase (2-hydroxylating)

Comments:

A flavoprotein (FAD).

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 91116-87-9

References:

1.	Mitra, D. and Vaidyanathan, C.S. A new 4-nitrophenol 2-hydroxylase from a Nocardia sp. Biochem. Int. 8 (1984) 609–615. [PMID: 6477623]

[EC 1.14.13.29 created 1989]

1.14.13.200

Accepted name:

tetracenomycin A2 monooxygenase-dioxygenase

Reaction:

tetracenomycin A2 + 2 O₂ + 2 NADPH + 2 H⁺ = tetracenomycin C + 2 NADP⁺ + H₂O

For diagram of tetracenomycin biosynthesis, 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,NADPH: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

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. [DOI] [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. [DOI] [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. [DOI] [PMID: 11092935]

[EC 1.14.13.200 created 2014]

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]

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]

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]

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]

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]

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]

1.14.13.207

Transferred entry:

ipsdienol synthase. Now EC 1.14.14.31, ipsdienol synthase

[EC 1.14.13.207 created 2015, deleted 2016]

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 Benzoyl-CoA catabolism, 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, PDB

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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 20452977]

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

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

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. [DOI] [PMID: 15006746]

[EC 1.14.13.209 created 2015]

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

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. [DOI] [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. [DOI] [PMID: 16751499]

[EC 1.14.13.210 created 2016]

1.14.13.211

Accepted name:

rifampicin monooxygenase

Reaction:

rifampicin + NAD(P)H + O₂ = 2-hydroxy-2,27-secorifampicin + NAD(P)⁺ + H₂O

For diagram of rifampicin, click here

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; ROX; RIFMO; rifampicin:NAD(P)H:oxygen oxidoreductase (2′-N-hydroxyrifampicin-forming) (incorrect)

Systematic name:

rifampicin:NAD(P)H:oxygen oxidoreductase (2-hydroxy-2,27-secorifampicin-forming; ring-cleaving)

Comments:

The enzyme has been found in a variety of environmental bacteria, notably Rhodococcus, Nocardia, and Streptomyces. It hydroxylates C-2 of rifampicin leading to its macro-ring cleaving.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

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. [DOI] [PMID: 19942945]
3.	Koteva, K., Cox, G., Kelso, J.K., Surette, M.D., Zubyk, H.L., Ejim, L., Stogios, P., Savchenko, A., Sørensen, D. and Wright, G.D. Rox, a rifamycin resistance enzyme with an unprecedented mechanism of action. Cell Chem Biol 25 (2018) 403–412.e5. [DOI] [PMID: 29398560]
4.	Liu, L.K., Dai, Y., Abdelwahab, H., Sobrado, P. and Tanner, J.J. Structural evidence for rifampicin monooxygenase inactivating rifampicin by cleaving Its ansa-bridge. Biochemistry 57 (2018) 2065–2068. [DOI] [PMID: 29578336]

[EC 1.14.13.211 created 2016, modified 2022]

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

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. [DOI] [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. [DOI] [PMID: 25678373]

[EC 1.14.13.212 created 2016]

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]

1.14.13.214

Transferred entry:

(–)-4′-demethyl-deoxypodophyllotoxin 4-hydroxylase. Now EC 1.14.14.132, (–)-4′-demethyl-deoxypodophyllotoxin 4-hydroxylase

[EC 1.14.13.214 created 2016, deleted 2018]

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

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. [DOI] [PMID: 23890006]

[EC 1.14.13.215 created 2016]

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

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. [DOI] [PMID: 23030663]

[EC 1.14.13.216 created 2016]

1.14.13.217

Accepted name:

protodeoxyviolaceinate monooxygenase

Reaction:

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

For diagram of violacein biosynthesis, 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, PDB

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. [DOI] [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. [DOI] [PMID: 17925955]

[EC 1.14.13.217 created 2016, modified 2016]

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 enediyne antitumour antibiotic biosynthesis and pyocyanin biosynthesis, click here

Glossary:

pyocyanin = 1-hydroxy-5-methylphenazin-5-ium

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 phenazin-1-ol.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

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. [DOI] [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. [DOI] [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. [DOI] [PMID: 18416536]

[EC 1.14.13.218 created 2016]

1.14.13.219

Accepted name:

resorcinol 4-hydroxylase (NADPH)

Reaction:

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

Glossary:

resorcinol = benzene-1,3-diol
hydroxyquinol = benzene-1,2,4-triol

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

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. [DOI] [PMID: 16963551]

[EC 1.14.13.219 created 2016]

1.14.13.220

Accepted name:

resorcinol 4-hydroxylase (NADH)

Reaction:

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

Glossary:

resorcinol = benzene-1,3-diol
hydroxyquinol = benzene-1,2,4-triol

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

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. [DOI] [PMID: 26319878]

[EC 1.14.13.220 created 2016]

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]

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

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

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. [DOI] [PMID: 22907798]

[EC 1.14.13.222 created 2016]

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

Glossary:

anthranilate = 2-aminobenzoate

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

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. [DOI] [PMID: 21612226]

[EC 1.14.13.223 created 2016]

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 violacein biosynthesis, click here

Glossary:

violacein = (3E)-3-[5-(5-hydroxy-1H-indol-3-yl)-2-oxo-1,2-dihydro-3H-pyrrol-3-ylidene]-1,3-dihydro-2H-indol-2-one

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

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. [DOI] [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. [DOI] [PMID: 17925955]

[EC 1.14.13.224 created 2016]

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, PDB

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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 26845023]

[EC 1.14.13.225 created 2016]

1.14.13.226

Accepted name:

acetone monooxygenase (methyl acetate-forming)

Reaction:

acetone + NADPH + H⁺ + O₂ = methyl acetate + NADP⁺ + H₂O

Other name(s):

acmA (gene name)

Systematic name:

acetone,NADPH:oxygen oxidoreductase (methyl acetate-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

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. [DOI] [PMID: 17071761]

[EC 1.14.13.226 created 2016]

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

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. [DOI] [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. [DOI] [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. [DOI] [PMID: 21183637]

[EC 1.14.13.227 created 2016]

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

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. [DOI] [PMID: 26258762]

[EC 1.14.13.228 created 2016]

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

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. [DOI] [PMID: 22194447]

[EC 1.14.13.229 created 2016]

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

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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 19383682]

[EC 1.14.13.230 created 2016]

1.14.13.231

Accepted name:

tetracycline 11a-monooxygenase

Reaction:

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

For diagram of tetracycline biosynthesis, 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, PDB

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. [DOI] [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. [DOI] [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. [DOI] [PMID: 21402075]

[EC 1.14.13.231 created 2016]

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 tetracycline biosynthesis, 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

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. [DOI] [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. [DOI] [PMID: 19472250]

[EC 1.14.13.232 created 2016]

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 tetracycline biosynthesis, 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

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. [DOI] [PMID: 18422316]

[EC 1.14.13.233 created 2016]

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 tetracycline biosynthesis, 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, PDB

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. [DOI] [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. [DOI] [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. [DOI] [PMID: 23621493]

[EC 1.14.13.234 created 2016]

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

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. [DOI] [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. [DOI] [PMID: 23881445]

[EC 1.14.13.235 created 2017]

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, PDB

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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 24798294]

[EC 1.14.13.236 created 2017]

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); ω-(methylthio)alkyl-glucosinolate,NADPH:oxygen S-oxidoreductase

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-(methylsulfanyl)octyl glucosinolate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

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. [DOI] [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. [DOI] [PMID: 18799661]

[EC 1.14.13.237 created 2017]

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

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. ISME J. 11 (2017) 1592–1601. [DOI] [PMID: 28304370]

[EC 1.14.13.238 created 2017]