Continued from EC 1.13.12 to EC 1.14.12
See separate file for EC 1.14.13.51 to EC 1.14.13.100
EC 1.14.13.101 to EC 1.14.13.150
EC 1.14.13.151 to EC 1.14.13.252
See the following files for:
EC 1.14.13.51 to EC 1.14.13.100
EC 1.14.13.101 to EC 1.14.13.150
EC 1.14.13.151 to EC 1.14.13.252
Accepted name: salicylate 1-monooxygenase
Reaction: salicylate + NADH + 2 H+ + O2 = catechol + NAD+ + H2O + CO2
For diagram of reaction click here or click here.
Other name(s): salicylate hydroxylase; salicylate 1-hydroxylase; salicylate monooxygenase; salicylate hydroxylase (decarboxylating)
Systematic name: salicylate,NADH:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9059-28-3
References:
1. Suzuki, K., Takemori, S. and Katagiri, M. Mechanism of the salicylate hydroxylase reaction. IV. Fluorimetric analysis of the complex formation. Biochim. Biophys. Acta 191 (1969) 77-85.
2. Takemori, S., Yasuda, H., Mihara, K., Suzuki, K. and Katagiri, M. Mechanism of the salicylate hydroxylase reaction. II. The enzyme-substrate complex. Biochim. Biophys. Acta 191 (1969) 58-68. [PMID: 4898626]
3. Takemori, S., Yasuda, H., Mihara, K., Suzuki, K. and Katagiri, M. Mechanism of the salicylate hydroxylase reaction. 3. Characterization and reactivity of chemically or photochemically reduced enzyme-flavin. Biochim. Biophys. Acta 191 (1969) 69-76. [PMID: 4309912]
4. Yamamoto, S., Katagiri, M., Maeno, H. and Hayaishi, O. Salicylate hydroxylase, a monooxygenase requiring flavin adenine dinucleotide. J. Biol. Chem. 240 (1965) 3408-3413.
Accepted name: 4-hydroxybenzoate 3-monooxygenase
Reaction: 4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
For diagram 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. [PMID: 8706756]
[EC 1.14.13.3 Transferred entry: 4-hydroxyphenylacetate 3-monooxygenase. Now EC 1.14.14.9, 4-hydroxyphenylacetate 3-monooxygenase. (EC 1.14.13.3 created 1972, deleted 2011)]
Accepted name: melilotate 3-monooxygenase
Reaction: 3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 = 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
Other name(s): 2-hydroxyphenylpropionate hydroxylase; melilotate hydroxylase; 2-hydroxyphenylpropionic hydroxylase; melilotic hydroxylase
Systematic name: 3-(2-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase (3-hydroxylating)
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-72-7
References:
1. Levy, C.C. Melilotate hydroxylase. Purification of the enzyme and the nature of the prosthetic group. J. Biol. Chem. 242 (1967) 747-753. [PMID: 6017743]
2. Levy, C.C. and Frost, P. The metabolism of coumarin by a microorganism. V. Melilotate hydroxylase. J. Biol. Chem. 241 (1966) 997-1003. [PMID: 4285850]
3. Strickland, S. and Massey, V. The purification and properties of the flavoprotein melilotate hydroxylase. J. Biol. Chem. 248 (1973) 2944-2952. [PMID: 4348920]
4. Strickland, S. and Massey, V. The mechanism of action of the flavoprotein melilotate hydroxylase. J. Biol. Chem. 248 (1973) 2953-2962. [PMID: 4348921]
Accepted name: imidazoleacetate 4-monooxygenase
Reaction: 4-imidazoleacetate + NADH + H+ + O2 = 5-hydroxy-4-imidazoleacetate + NAD+ + H2O
Other name(s): imidazoleacetic hydroxylase; imidazoleacetate hydroxylase; imidazoleacetic monooxygenase
Systematic name: 4-imidazoleacetate,NADH:oxygen oxidoreductase (5-hydroxylating)
Comments: A flavoprotein (FAD). Formerly EC 1.14.1.5.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-65-6
References:
1. Maki, Y., Yamamoto, S., Nozaki, M. and Hayaishi, O. Studies on monooxygenases. II. Crystallization and some properties of imidazole acetate monooxygenase. J. Biol. Chem. 244 (1969) 2942-2950. [PMID: 5772468]
Accepted name: orcinol 2-monooxygenase
Reaction: orcinol + NADH + H+ + O2 = 2,3,5-trihydroxytoluene + NAD+ + H2O
Other name(s): orcinol hydroxylase
Systematic name: orcinol,NADH:oxygen oxidoreductase (2-hydroxylating)
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 37217-34-8
References:
1. Otha, Y. and Ribbons, D.W. Crystallization of orchinol hydroxylase from Pseudomonas putida. FEBS Lett. 11 (1970) 189-192.
Accepted name: phenol 2-monooxygenase (NADPH)
Reaction: phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O
For diagram of reaction click here.
Glossary: o-cresol = 2-cresol = 2-methylphenol
Other name(s): phenol hydroxylase; phenol o-hydroxylase
Systematic name: phenol,NADPH:oxygen oxidoreductase (2-hydroxylating)
Comments: A flavoprotein (FAD). The enzyme from the fungus Trichosporon cutaneum has a broad substrate specificity, and has been reported to catalyse the hydroxylation of a variety of substituted phenols, such as fluoro-, chloro-, amino- and methyl-phenols and also dihydroxybenzenes. cf. EC 1.14.14.20, phenol 2-monooxygenase (FADH2).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-84-1
References:
1. Nakagawa, H. and Takeda, Y. Phenol hydroxylase. Biochim. Biophys. Acta 62 (1962) 423-426. [PMID: 14478080]
2. Neujahr, H.Y. and Gaal, A. Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum, Eur. J. Biochem. 35 (1973) 386-400. [PMID: 4146224]
3. Neujahr, H.Y. and Gaal, A. Phenol hydroxylase from yeast. Sulfhydryl groups in phenol hydroxylase from Trichosporon cutaneum, Eur. J. Biochem. 58 (1975) 351-357. [PMID: 810352]
Accepted name: flavin-containing monooxygenase
Reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
Other name(s): dimethylaniline oxidase; dimethylaniline N-oxidase; FAD-containing monooxygenase; N,N-dimethylaniline monooxygenase; DMA oxidase; flavin mixed function oxidase; Ziegler's enzyme; mixed-function amine oxidase; FMO; FMO-I; FMO-II; FMO1; FMO2; FMO3; FMO4; FMO5; flavin monooxygenase; methylphenyltetrahydropyridine N-monooxygenase; 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine:oxygen N-oxidoreductase; dimethylaniline monooxygenase (N-oxide-forming)
Systematic name: N,N-dimethylaniline,NADPH:oxygen oxidoreductase (N-oxide-forming)
Comments: A flavoprotein. A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines [3,4]. This enzyme is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate [4,5]. This microsomal enzyme generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites. For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) [2,6]
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37256-73-8
References:
1. Ziegler, D.M. and Pettit, F.H. Microsomal oxidases. I. The isolation and dialkylarylamine oxygenase activity of pork liver microsomes. Biochemistry 5 (1966) 2932-2938. [PMID: 4381353]
2. Chiba, K., Kubota, E., Miyakawa, T., Kato, Y. and Ishizaki, T. Characterization of hepatic microsomal metabolism as an in vivo detoxication pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine in mice. J. Pharmacol. Exp. Ther. 246 (1988) 1108-1115. [PMID: 3262153]
3. Cashman, J.R. Structural and catalytic properties of the mammalian flavin-containing monooxygenase. Chem. Res. Toxicol. 8 (1995) 165-181.
4. Cashman, J.R. and Zhang, J. Human flavin-containing monooxygenases. Annu. Rev. Pharmacol. Toxicol. 46 (2006) 65-100. [PMID: 16402899]
5. Jones, K.C. and Ballou, D.P. Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates. J. Biol. Chem. 261 (1986) 2553-2559. [PMID: 3949735]
6. Chiba, K., Kobayashi, K., Itoh, K., Itoh, S., Chiba, T., Ishizaki, T. and Kamataki, T. N-Oxygenation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine by the rat liver flavin-containing monooxygenase expressed in yeast cells. Eur. J. Pharmacol. 293 (1995) 97-100. [PMID: 7672012]
Accepted name: kynurenine 3-monooxygenase
Reaction: L-kynurenine + NADPH + H+ + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O
For diagram of reaction click here.
Other name(s): kynurenine 3-hydroxylase; kynurenine hydroxylase; L-kynurenine-3-hydroxylase
Systematic name: L-kynurenine,NADPH:oxygen oxidoreductase (3-hydroxylating)
Comments: A flavoprotein (FAD). Formerly EC 1.14.1.2 and EC 1.99.1.5.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-61-2
References:
1. de Castro, F.T., Price, J.M. and Brown, R.R. Reduced triphosphopyridinenucleotide requirement for the enzymatic formation of 3-hydroxykynurenine from L-kynurenine. J. Am. Chem. Soc. 78 (1956) 2904-2905.
2. Okamoto, H. and Hayaishi, O. Flavin adenine dinucleotide requirement for kynurenine hydroxylase of rat liver mitochondria. Biochem. Biophys. Res. Commun. 29 (1967) 394-399. [PMID: 6076241]
3. Saito, Y., Hayaishi, O. and Rothberg, S. Studies on oxygenases: enzymatic formation of 3-hydroxy-L-kynurenine from L-kynurenine. J. Biol. Chem. 229 (1957) 921-934.
Accepted name: 2,6-dihydroxypyridine 3-monooxygenase
Reaction: 2,6-dihydroxypyridine + NADH + H+ + O2 = 2,3,6-trihydroxypyridine + NAD+ + H2O
For diagram of reaction click here.
Other name(s): 2,6-dihydroxypyridine oxidase
Systematic name: 2,6-dihydroxypyridine,NADH:oxygen oxidoreductase (3-hydroxylating)
Comments: A flavoprotein.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 39279-38-4
References:
1. Holmes, P.E. and Rittenberg, S.C. The bacterial oxidation of nicotine. VII. Partial purification and properties of 2,6-dihydroxypyridine oxidase. J. Biol. Chem. 247 (1972) 7622-7627. [PMID: 4344227]
2. Holmes, P.E., Rittenberg, S.C. and Knackmuss, H.J. The bacterial oxidation of nicotine. 8. Synthesis of 2,3,6-trihydroxypyridine and accumulation and partial characterization of the product of 2,6-dihydroxypyridine oxidation. J. Biol. Chem. 247 (1972) 7628-7633. [PMID: 4636328]
[EC 1.14.13.11 Transferred entry: trans-cinnamate 4-monooxygenase. Now EC 1.14.14.91, trans-cinnamate 4-monooxygenase (EC 1.14.13.11 created 1976, deleted 2018)]
[EC 1.14.13.12 Transferred entry: benzoate 4-monooxygenase. Now EC 1.14.14.92, benzoate 4-monooxygenase (EC 1.14.13.12 created 1976, deleted 2018)]
[EC 1.14.13.13 Transferred entry: calcidiol 1-monooxygenase, Now classified as EC 1.14.15.18, calcidiol 1-monooxygenase (EC 1.14.13.13 created 1976, deleted 2016)]
Accepted name: trans-cinnamate 2-monooxygenase
Reaction: trans-cinnamate + NADPH + H+ + O2 = 2-hydroxycinnamate + NADP+ + H2O
Other name(s): cinnamic acid 2-hydroxylase; cinnamate 2-monooxygenase; cinnamic 2-hydroxylase; cinnamate 2-hydroxylase; trans-cinnamic acid 2-hydroxylase
Systematic name: trans-cinnamate,NADPH:oxygen oxidoreductase (2-hydroxylating)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 53126-56-0
References:
1. Gestetner, B. and Conn, E.E. The 2-hydroxylation of trans-cinnamic acid by chloroplasts from Melilotus alba Desr. Arch. Biochem. Biophys. 163 (1974) 617-624. [PMID: 4153528]
[EC 1.14.13.15 Transferred entry: cholestanetriol 26-monooxygenase, now classified as EC 1.14.15.15, cholestanetriol 26-monooxygenase. (EC 1.14.13.15 created 1976, modified 2005, modified 2012, deleted 2016)]
Accepted name: cyclopentanone monooxygenase
Reaction: cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O
Other name(s): cyclopentanone oxygenase
Systematic name: cyclopentanone,NADPH:oxygen oxidoreductase (5-hydroxylating, lactonizing)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37364-15-1
References:
1. Griffin, M. and Trudgill, P.W. The metabolism of cyclopentanol by Pseudomonas N.C.I.B. 9872. Biochem. J. 129 (1972) 595-603. [PMID: 4349113]
2. Griffin, M. and Trudgill, P.W. Purification and properties of cyclopentanone oxygenase of Pseudomonas NCIB 9872. Eur. J. Biochem. 63 (1976) 199-209. [PMID: 4313]
[EC 1.14.13.17 Transferred entry: cholesterol 7α-monooxygenase, now classified as EC 1.14.14.23, cholesterol 7α-monooxygenase (EC 1.14.13.17 created 1976, deleted 2016)]
Accepted name: 4-hydroxyphenylacetate 1-monooxygenase
Reaction: 4-hydroxyphenylacetate + NAD(P)H + H+ + O2 = homogentisate + NAD(P)+ + H2O
For diagram of reaction click here.
Other name(s): 4-hydroxyphenylacetate 1-hydroxylase; 4-hydroxyphenylacetic 1-hydroxylase; 4-HPA 1-hydroxylase
Systematic name: 4-hydroxyphenylacetate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating)
Comments: A flavoprotein (FAD). Also acts on 4-hydroxyhydratropate (forming 2-methylhomogentisate) and on 4-hydroxyphenoxyacetate (forming hydroquinone and glycolate).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 55326-44-8
References:
1. Hareland, W.A., Crawford, R.L., Chapman, P.J. and Dagley, S. Metabolic function and properties of 4-hydroxyphenylacetic acid 1-hydroxylase from Pseudomonas acidovorans. J. Bacteriol. 121 (1975) 272-285. [PMID: 234937]
Accepted name: taxifolin 8-monooxygenase
Reaction: taxifolin + NAD(P)H + H+ + O2 = 2,3-dihydrogossypetin + NAD(P)+ + H2O
Other name(s): taxifolin hydroxylase
Systematic name: taxifolin,NAD(P)H:oxygen oxidoreductase (8-hydroxylating)
Comments: A flavoprotein, converting a flavanol into a flavanone. Also acts on fustin, but not on catechin, quercetin or mollisacidin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 39307-19-2
References:
1. Jeffrey, A.M., Knight, M. and Evans, W.C. The bacterial degradation of flavonoids. Hydroxylation of the A-ring of taxifolin by a soil pseudomonad. Biochem. J. 130 (1972) 373-381. [Medline UI: 4146277]
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. [PMID: 7075592]
[EC 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)]
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. [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. [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. [PMID: ]
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. Formerly EC 1.14.99.13.
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. [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]
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. [PMID: 4357436]
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. [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 1.14.13.26 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)]
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 1.14.13.28 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)]
Accepted name: 4-nitrophenol 2-monooxygenase
Reaction: 4-nitrophenol + NADH + H+ + O2 = 4-nitrocatechol + NAD+ + H2O
For diagram of reaction 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 1.14.13.30 Transferred entry: leukotriene-B4 20-monooxygenase. Now EC 1.14.14.94, leukotriene-B4 20-monooxygenase (EC 1.14.13.30 created 1989, deleted 2018)]
Accepted name: 2-nitrophenol 2-monooxygenase
Reaction: 2-nitrophenol + NADPH + H+ + O2 = catechol + nitrite + NADP+ + H2O
For diagram of reaction click here.
Other name(s): 2-nitrophenol oxygenase; nitrophenol oxygenase
Systematic name: 2-nitrophenol,NADPH:oxygen 2-oxidoreductase (2-hydroxylating, nitrite-forming)
Comments: Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 104520-84-5
References:
1. Zeyer, J., Kocher, H.P. and Timmis, N. Influence of para-substituents on the oxidative metabolism of o-nitrophenols by Pseudomonas putida B2. Appl. Environ. Microbiol. 52 (1986) 334-339. [PMID: 3752997]
Accepted name: albendazole monooxygenase
Reaction: albendazole + NADPH + H+ + O2 = albendazole S-oxide + NADP+ + H2O
For diagram of reaction click here.
Glossary: albendazole = methyl [5-(propylsulfanyl)-1H-benzimidazol-2-yl]carbamate
Other name(s): albendazole oxidase (misleading); albendazole sulfoxidase (ambiguous); FMO3 (gene name); albendazole monooxygenase (flavin-containing)
Systematic name: albendazole,NADPH:oxygen oxidoreductase (sulfoxide-forming)
Comments: A microsomal flavin-containing monooxygenase. A similar conversion is also carried out by some microsomal cytochrome P-450 enzymes [EC 1.14.14.73, albendazole monooxygenase (sulfoxide-forming)]. It is estimated that cytochrome P-450s are responsible for 70% of the activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 101299-59-6
References:
1. Fargetton, X., Galtier, P. and Delatour, P. Sulfoxidation of albendazole by a cytochrome P450-independent monooxygenase from rat liver microsomes. Vet. Res. Commun. 10 (1986) 317-324. [PMID: 3739217]
2. Moroni, P., Buronfosse, T., Longin-Sauvageon, C., Delatour, P. and Benoit, E. Chiral sulfoxidation of albendazole by the flavin adenine dinucleotide-containing and cytochrome P450-dependent monooxygenases from rat liver microsomes. Drug Metab. Dispos. 23 (1995) 160-165. [PMID: 7736906]
3. Rawden, H.C., Kokwaro, G.O., Ward, S.A. and Edwards, G. Relative contribution of cytochromes P-450 and flavin-containing monoxygenases to the metabolism of albendazole by human liver microsomes. Br. J. Clin. Pharmacol. 49 (2000) 313-322. [PMID: 10759686]
Accepted name: 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]
Reaction: 4-hydroxybenzoate + NAD(P)H + H+ + O2 = 3,4-dihydroxybenzoate + NAD(P)+ + H2O
Other name(s): 4-hydroxybenzoate 3-monooxygenase (reduced nicotinamide adenine dinucleotide (phosphate)); 4-hydroxybenzoate-3-hydroxylase; 4-hydroxybenzoate 3-hydroxylase
Systematic name: 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (3-hydroxylating)
Comments: A flavoprotein (FAD). The enzyme from Corynebacterium cyclohexanicum is highly specific for 4-hydroxybenzoate, but uses NADH and NADPH at approximately equal rates (cf. EC 1.14.13.2 4-hydroxybenzoate 3-monooxygenase). It is less specific for NADPH than EC 1.14.13.2.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 95471-33-3
References:
1. Fujii, T. and Kaneda, T. Purification and properties of NADH/NADPH-dependent p-hydroxybenzoate hydroxylase from Corynebacterium cyclohexanicum. Eur. J. Biochem. 147 (1985) 97-104. [PMID: 3971979]
2. 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. [PMID: 8706756]
Accepted name: leukotriene-E4 20-monooxygenase
Reaction: (7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14-tetraenoate + NADPH + H+ + O2 = 20-hydroxyleukotriene E4 + NADP+ + H2O
Other name(s): leukotriene-E4 ω-hydroxylase
Systematic name: (7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14-tetraenoate,NADPH:oxygen oxidoreductase (20-hydroxylating)
Comments: Also acts on N-acetyl-leucotriene E4, but more slowly. Not identical with EC 1.14.13.30 leukotriene-B4 20-monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 111940-51-3
References:
1. Örning, L. ω-Oxidation of cysteine-containing leukotrienes by rat-liver microsomes. Isolation and characterization of ω-hydroxy and ω-carboxy metabolites of leukotriene E4 and N-acetylleukotriene E4. Eur. J. Biochem. 170 (1987) 77-85. [PMID: 2826163]
Accepted name: anthranilate 3-monooxygenase (deaminating)
Reaction: anthranilate + NADPH + H+ + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3
Other name(s): anthranilate hydroxylase; anthranilate 2,3-dioxygenase (deaminating); anthranilate hydroxylase (deaminating); anthranilic hydroxylase; anthranilate 2,3-hydroxylase (deaminating)
Systematic name: anthranilate,NADPH:oxygen oxidoreductase (3-hydroxylating, deaminating)
Comments: The enzyme from Aspergillus niger is an iron protein; that from the yeast Trichosporon cutaneum is a flavoprotein (FAD). Previously EC 1.14.12.2.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 37256-68-1
References:
1. Powlowski, J.B., Dagley, S., Massey, V. and Ballou, D.P. Properties of anthranilate hydroxylase (deaminating), a flavoprotein from Trichosporon cutaneum. J. Biol. Chem. 262 (1987) 69-74. [PMID: 3793735]
2. Subramanian, V. and Vaidyanathan, C.S. Anthranilate hydroxylase from Aspergillus niger: new type of NADPH-linked nonheme iron monooxygenase. J. Bacteriol. 160 (1984) 651-655. [PMID: 6501219]
[EC 1.14.13.36 Transferred entry: 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase. Now EC 1.14.14.96, 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase (EC 1.14.13.36 created 1990, deleted 2018)]
[EC 1.14.13.37 Transferred entry: methyltetrahydroprotoberberine 14-monooxygenase. Now EC 1.14.14.97, methyltetrahydroprotoberberine 14-monooxygenase (EC 1.14.13.37 created 1990, deleted 2018)]
Accepted name: anhydrotetracycline 6-monooxygenase
Reaction: anhydrotetracycline + NADPH + H+ + O2 = 12-dehydrotetracycline + NADP+ + H2O
For diagram of reaction click here.
Glossary: anhydrotetracycline = (4S,4aS,12aS)-4-(dimethylamino)-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-1,4,4a,5,12,12a-hexahydrotetracene-2-carboxamide
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): ATC oxygenase; anhydrotetracycline oxygenase; oxyS (gene name); anhydrotetracycline monooxygenase
Systematic name: anhydrotetracycline,NADPH:oxygen oxidoreductase (6-hydroxylating)
Comments: The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. It can also catalyse EC 1.14.13.234, 12-dehydrotetracycline 5-monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 70766-62-0
References:
1. Behal, V., Hostalek, Z. and Vanek, Z. Anhydrotetracycline oxygenase activity and biosynthesis of tetracyclines in streptomyces aureofaciens. Biotechnol. Lett. 1 (1979) 177-182.
2. 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]
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]
Accepted name: nitric-oxide synthase (NADPH)
Reaction: 2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O (overall reaction)
(1a) 2 L-arginine + 2 NADPH + 2 H+ + 2 O2 = 2 Nω-hydroxy-L-arginine + 2 NADP+ + 2 H2O
(1b) 2 Nω-hydroxy-L-arginine + NADPH + H+ + 2 O2 = 2 L-citrulline + 2 nitric oxide + NADP+ + 2 H2O
Glossary: nitric oxide = NO = nitrogen(II) oxide
Other name(s): NOS (gene name); nitric oxide synthetase (ambiguous); endothelium-derived relaxation factor-forming enzyme; endothelium-derived relaxing factor synthase; NO synthase (ambiguous); NADPH-diaphorase (ambiguous)
Systematic name: L-arginine,NADPH:oxygen oxidoreductase (nitric-oxide-forming)
Comments: The enzyme consists of linked oxygenase and reductase domains. The eukaryotic enzyme binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin, and its two domains are linked via a regulatory calmodulin-binding domain. Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. The reductase domain of the enzyme from the bacterium Sorangium cellulosum utilizes a [2Fe-2S] cluster to transfer the electrons from NADPH to the active center. cf. EC 1.14.14.47, nitric-oxide synthase (flavodoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 125978-95-2
References:
1. Bredt, D.S. and Snyder, S.H. Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme. Proc. Natl. Acad. Sci. USA 87 (1990) 682-685. [PMID: 1689048]
2. Stuehr, D.J., Kwon, N.S., Nathan, C.F., Griffith, O.W., Feldman, P.L. and Wiseman, J. Nω-hydroxy-L-arginine is an intermediate in the biosynthesis of nitric oxide from L-arginine. J. Biol. Chem. 266 (1991) 6259-6263. [PMID: 1706713]
3. Stuehr, D., Pou, S. and Rosen, G.M. Oxygen reduction by nitric-oxide synthases. J. Biol. Chem. 276 (2001) 14533-14536. [PMID: 11279231]
4. Agapie, T., Suseno, S., Woodward, J.J., Stoll, S., Britt, R.D. and Marletta, M.A. NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum. Proc. Natl. Acad. Sci. USA 106 (2009) 16221-16226. [PMID: 19805284]
5. Foresi, N., Correa-Aragunde, N., Parisi, G., Calo, G., Salerno, G. and Lamattina, L. Characterization of a nitric oxide synthase from the plant kingdom: NO generation from the green alga Ostreococcus tauri is light irradiance and growth phase dependent. Plant Cell 22 (2010) 3816-3830. [PMID: 21119059]
Accepted name: anthraniloyl-CoA monooxygenase
Reaction: anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
Glossary: anthraniloyl-CoA = 2-aminobenzoyl-CoA
Other name(s): anthraniloyl coenzyme A reductase; 2-aminobenzoyl-CoA monooxygenase/reductase; 2-aminobenzoyl-CoA,NAD(P)H:oxygen oxidoreductase (de-aromatizing)
Systematic name: anthraniloyl-CoA,NAD(P)H:oxygen oxidoreductase (de-aromatizing)
Comments: A flavoprotein (FAD). The non-aromatic product is unstable and releases CO2 and NH3, forming 1,4-cyclohexanedione.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 112692-57-6
References:
1. Buder, R. and Fuchs, G. 2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Purification and some properties of the enzyme. Eur. J. Biochem. 185 (1989) 629-635. [PMID: 2591379]
2. Buder, R., Ziegler, K., Fuchs, G., Langkau, B. and Ghisla, S. 2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Studies on the stoichiometry and the course of the reaction. Eur. J. Biochem. 185 (1989) 637-643. [PMID: 2591380]
3. Langkau, B., Ghisla, S., Buder, R., Ziegler, K. and Fuchs, G. 2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Identification of the reaction products. Eur. J. Biochem. 191 (1990) 365-371. [PMID: 2384085]
[EC 1.14.13.41 Transferred entry: tyrosine N-monooxygenase. Now EC 1.14.14.36, tyrosine N-monooxygenase (EC 1.14.13.41 created 1992, modified 2001, modified 2005, deleted 2016)]
[EC 1.14.13.42 Deleted entry: hydroxyphenylacetonitrile 2-monooxygenase. The activity is covered by EC 1.14.13.68, 4-hydroxyphenylacetaldehyde oxime monooxygenase, that performs the two consecutive reactions in the conversion of (Z)-4-hydroxyphenylacetaldehyde oxime to (S)-4-hydroxymandelonitrile (EC 1.14.13.42 created 1992, deleted 2011)]
Accepted name: questin monooxygenase
Reaction: questin + NADPH + H+ + O2 = demethylsulochrin + NADP+
Glossary: questin = 3,8-dihydroxy-1-methoxy-6-methylanthracene-9,10-dione
demethylsulochrin = 2-(2,6-dihydroxy-4-methylbenzoyl)-5-hydroxy-3-methoxybenzoic acid
Other name(s): questin oxygenase
Systematic name: questin,NADPH:oxygen oxidoreductase (hydroxylating, anthraquinone-ring-opening)
Comments: The enzyme cleaves the anthraquinone ring of questin to form a benzophenone. Involved in the biosynthesis of the seco-anthraquinone (+)-geodin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 115232-45-6
References:
1. Fujii, I., Ebizuka, Y. and Sankawa, U. A novel anthraquinone ring cleavage enzyme from Aspergillus terreus. J. Biochem. (Tokyo) 103 (1988) 878-883. [PMID: 3182756]
Accepted name: 2-hydroxybiphenyl 3-monooxygenase
Reaction: 2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ + H2O
Systematic name: 2-hydroxybiphenyl,NADH:oxygen oxidoreductase (3-hydroxylating)
Comments: Also converts 2,2'-dihydroxybiphenyl into 2,2',3-trihydroxy-biphenyl.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 118251-39-1
References:
1. Kohler, H.-P.E., Kohler-Staub, D. and Focht, D.D. Degradation of 2-hydroxybiphenyl and 2,2'-dihydroxybiphenyl by Pseudomonas sp. strain HBP1. Appl. Environ. Microbiol. 54 (1988) 2683-2688. [PMID: 3214154]
[EC 1.14.13.45 Transferred entry: now EC 1.14.18.2 CMP-N-acetylneuraminate monooxygenase. (EC 1.14.13.45 created 1992, deleted 2003)]
Accepted name: (–)-menthol monooxygenase
Reaction: (–)-menthol + NADPH + H+ + O2 = p-menthane-3,8-diol + NADP+ + H2O
For diagram of reaction click here.
Other name(s): l-menthol monooxygenase
Systematic name: (–)-menthol,NADPH:oxygen oxidoreductase (8-hydroxylating)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 117590-75-7
References:
1. Madyastha, K.M. and Srivatsan, V. Studies on the metabolism of l-menthol in rats. Drug Metab. Dispos. 16 (1988) 765-772. [PMID: 2906604]
[EC 1.14.13.47 Transferred entry: (S)-limonene 3-monooxygenase. Now EC 1.14.14.99, (S)-limonene 3-monooxygenase (EC 1.14.13.47 created 1992, modified 2003, deleted 2018)]
[EC 1.14.13.48 Transferred entry: (S)-limonene 6-monooxygenase. Now classified as EC 1.14.14.51, (S)-limonene 6-monooxygenase (EC 1.14.13.48 created 1992, modified 2003, deleted 2017)]
[EC 1.14.13.49 Transferred entry: (S)-limonene 7-monooxygenase. Now classified as EC 1.14.14.52, (S)-limonene 7-monooxygenase (EC 1.14.13.49 created 1992, modified 2003, deleted 2017)]
Accepted name: pentachlorophenol monooxygenase
Reaction: (1) pentachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
(2) 2,3,5,6-tetrachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachlorohydroquinone + NADP+ + H2O
Other name(s): pcpB (gene name); pentachlorophenol dechlorinase; pentachlorophenol dehalogenase; pentachlorophenol 4-monooxygenase; PCP hydroxylase; pentachlorophenol hydroxylase; PCB 4-monooxygenase; PCB4MO
Systematic name: pentachlorophenol,NADPH:oxygen oxidoreductase (hydroxylating, dechlorinating)
Comments: A flavoprotein (FAD). The enzyme displaces a diverse range of substituents from the 4-position of polyhalogenated phenols but requires that a halogen substituent be present at the 2-position [2]. If C-4 carries a halogen substituent, reaction 1 is catalysed; if C-4 is unsubstituted, reaction 2 is catalysed.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 136111-57-4
References:
1. Schenk, T., Müller, R., Mörsberger, F., Otto, M.K. and Lingens, F. Enzymatic dehalogenation of pentachlorophenol by extracts from Arthrobacter sp. strain ATCC 33790. J. Bacteriol. 171 (1989) 5487-5491. [PMID: 2793827]
2. Xun, L., Topp, E. and Orser, C.S. Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries. J. Bacteriol. 174 (1992) 2898-2902. [PMID: 1569020]
3. Xun, L., Topp, E. and Orser, C.S. Confirmation of oxidative dehalogenation of pentachlorophenol by a Flavobacterium pentachlorophenol hydroxylase. J. Bacteriol. 174 (1992) 5745-5747. [PMID: 1512208]
4. Lange, C.C., Schneider, B.J. and Orser, C.S. Verification of the role of PCP 4-monooxygenase in chlorine elimination from pentachlorophenol by Flavobacterium sp. strain ATCC 39723. Biochem. Biophys. Res. Commun. 219 (1996) 146-149. [PMID: 8619798]
5. Nakamura, T., Motoyama, T., Hirono, S. and Yamaguchi, I. Identification, characterization, and site-directed mutagenesis of recombinant pentachlorophenol 4-monooxygenase. Biochim. Biophys. Acta 1700 (2004) 151-159. [PMID: 15262224]
6. Chen, L. and Yang, J. Biochemical characterization of the tetrachlorobenzoquinone reductase involved in the biodegradation of pentachlorophenol. Int J Mol Sci 9 (2008) 198-212. [PMID: 19325743]
7. Hlouchova, K., Rudolph, J., Pietari, J.M., Behlen, L.S. and Copley, S.D. Pentachlorophenol hydroxylase, a poorly functioning enzyme required for degradation of pentachlorophenol by Sphingobium chlorophenolicum. Biochemistry 51 (2012) 3848-3860. [PMID: 22482720]
8. Rudolph, J., Erbse, A.H., Behlen, L.S. and Copley, S.D. A radical intermediate in the conversion of pentachlorophenol to tetrachlorohydroquinone by Sphingobium chlorophenolicum. Biochemistry 53 (2014) 6539-6549. [PMID: 25238136]