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 1.14.13.171
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 1.14.13.171
Accepted name: salicylate 1-monooxygenase
Reaction: salicylate + NADH + 2 H+ + O2 = catechol + NAD+ + H2O + CO2
For diagram of reaction 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, EXPASY, KEGG, Metacyc, UM-BBD, 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 = protocatechuate + NADP+ + H2O
For diagram click here.
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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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, EXPASY, KEGG, Metacyc, UM-BBD, 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
Reaction: phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O
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). Also active with resorcinol and 2-methylphenol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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, 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, 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, EXPASY, KEGG, Metacyc, UM-BBD, 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]
Accepted name: trans-cinnamate 4-monooxygenase
Reaction: trans-cinnamate + NADPH + H+ + O2 = 4-hydroxycinnamate + NADP+ + H2O
For diagram click here.
Other name(s): cinnamic acid 4-hydroxylase; oxygenase, cinnamate 4-mono-; CA4H ; cytochrome P450 cinnamate 4-hydroxylase; cinnamate 4-hydroxylase; cinnamate 4-monooxygenase; cinnamate hydroxylase; cinnamic 4-hydroxylase; cinnamic acid 4-monooxygenase; cinnamic acid p-hydroxylase; hydroxylase, cinnamate 4-; t-cinnamic acid hydroxylase; trans-cinnamate 4-hydroxylase; trans-cinnamic acid 4-hydroxylase
Systematic name: trans-cinnamate,NADPH:oxygen oxidoreductase (4-hydroxylating)
Comments: NADH also acts, more slowly. Involves a heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9077-75-2
References:
1. Potts, J.R.M., Weklych, R. and Conn, E.E. The 4-hydroxylation of cinnamic acid by sorghum microsomes and the requirement for cytochrome P-450. J. Biol. Chem. 249 (1974) 5019-5026. [PMID: 4153152]
2. Russell, D.W. and Conn, E.E. The cinnamic acid 4-hydroxylase of pea seedlings. Arch. Biochem. Biophys. 122 (1967) 256-268. [PMID: 4383827]
Accepted name: benzoate 4-monooxygenase
Reaction: benzoate + NADPH + H+ + O2 = 4-hydroxybenzoate + NADP+ + H2O
For diagram click here.
Other name(s): benzoic acid 4-hydroxylase; benzoate 4-hydroxylase; benzoic 4-hydroxylase; benzoate-p-hydroxylase; p-hydroxybenzoate hydroxylase
Systematic name: benzoate,NADPH:oxygen oxidoreductase (4-hydroxylating)
Comments: Requires Fe2+ and tetrahydropteridine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 39391-25-8
References:
1. Reddy, C.C. and Vaidyanathan, C.S. Purification, properties and induction of a specific benzoate-4-hydroxylase from Aspergillus niger (UBC 814). Biochim. Biophys. Acta 384 (1975) 46-57. [PMID: 236777]
Accepted name: calcidiol 1-monooxygenase
Reaction: calcidiol + NADPH + H+ + O2 = calcitriol + NADP+ + H2O
For diagram of reaction click here.
Glossary: calcidiol = (3S,5Z,7E)-9,10-seco-5,7,10(19)-cholestatriene-3,25-diol
calcitriol = (1S,3R,5Z,7E)-9,10-seco-5,7,10(19)-cholestatriene-1,3,25-triol
Other name(s): 25-hydroxycholecalciferol 1-hydroxylase; 25-hydroxycholecalciferol 1-monooxygenase; 1-hydroxylase-25-hydroxyvitamin D3; 25-hydroxy D3-1α-hydroxylase; 25-hydroxycholecalciferol 1α-hydroxylase; 25-hydroxyvitamin D3 1α-hydroxylase
Systematic name: calcidiol,NADPH:oxygen oxidoreductase (1-hydroxylating)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9081-36-1
References:
1. Gray, R.W., Omdahl, J.L., Ghazarian, J.G. and De Luca, H.F. 25-Hydroxycholecalciferol-1-hydroxylase. Subcellular location and properties. J. Biol. Chem. 247 (1972) 7528-7532. [PMID: 4404596]
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]
Accepted name: cholestanetriol 26-monooxygenase
Reaction: 5β-cholestane-3α,7α,12α-triol + 3 NADPH + 3 H+ + 3 O2 = (25R)-3α,7α,12α-trihydroxy-5β-cholestan-26-oate + 3 NADP+ + 4 H2O (overall reaction)
(1a) 5β-cholestane-3α,7α,12α-triol + NADPH + H+ + O2 = (25R)-5β-cholestane-3α,7α,12α,26-tetraol + NADP+ + H2O
(1b) (25R)-5β-cholestane-3α,7α,12α,26-tetraol + NADPH + H+ + O2 = (25R)-3α,7α,12α-trihydroxy-5β-cholestan-26-al + NADP+ + 2 H2O
(1c) (25R)-3α,7α,12α-trihydroxy-5β-cholestan-26-al + NADPH+ + H+ + O2 = (25R)-3α,7α,12α-trihydroxy-5β-cholestan-26-oate + NADP+ + H2O
For diagram of reaction, click here
Other name(s): 5β-cholestane-3α,7α,12α-triol 26-hydroxylase; 5β-cholestane-3α,7α,12α-triol hydroxylase; cholestanetriol 26-hydroxylase; sterol 27-hydroxylase; sterol 26-hydroxylase; cholesterol 27-hydroxylase; CYP27A; CYP27A1; cytochrome P450 27A1'
Systematic name: 5β-cholestane-3α,7α,12α-triol,NADPH:oxygen oxidoreductase (26-hydroxylating)
Comments: The enzyme requires ferredoxin and ferredoxin reductase. It catalyses the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway. Can also act on cholesterol, cholest-5-en-3β,7α-diol, 7α-hydroxycholest-4-en-3-one, and 5β-cholestane-3α,7α-diol. The enzyme can also hydroxylate cholesterol at positions 24 and 25.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 52227-77-7
References:
1. Masui, T., Herman, R. and Staple, E. The oxidation of 5β-cholestane-3α,7α,12α,26-tetraol to 5β-cholestane-3α,7α,12α-triol-26-oic acid via 5β-cholestane-3α,7α,12α-triol-26-al by rat liver. Biochim. Biophys. Acta 117 (1966) 266-268. [PMID: 5914340]
2. Okuda, K. and Hoshita, N. Oxidation of 5β-cholestane-3α,7α,12α-triol by rat-liver mitochondria. Biochim. Biophys. Acta 164 (1968) 381-388. [PMID: 4388637]
3. Wikvall, K. Hydroxylations in biosynthesis of bile acids. Isolation of a cytochrome P-450 from rabbit liver mitochondria catalyzing 26-hydroxylation of C27-steroids. J. Biol. Chem. 259 (1984) 3800-3804. [PMID: 6423637]
4. Andersson, S., Davis, D.L., Dahlbäck, H., Jörnvall, H. and Russell, D.W. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem. 264 (1989) 8222-8229. [PMID: 2722778]
5. Dahlback, H. and Holmberg, I. Oxidation of 5β-cholestane-3α,7α,12α-triol into 3α,7α,12α-trihydroxy-5β-cholestanoic acid by cytochrome P-45026 from rabbit liver mitochondria. Biochem. Biophys. Res. Commun. 167 (1990) 391-395. [PMID: 2322231]
6. Holmberg-Betsholtz, I., Lund, E., Björkhem, I. and Wikvall, K. Sterol 27-hydroxylase in bile acid biosynthesis. Mechanism of oxidation of 5β-cholestane-3α,7α,12α,27-tetrol into 3α,7α,12α-trihydroxy-5β-cholestanoic acid. J. Biol. Chem. 268 (1993) 11079-11085. [PMID: 8496170]
7. Pikuleva, I.A., Babiker, A., Waterman, M.R. and Bjorkhem, I. Activities of recombinant human cytochrome P450c27 (CYP27) which produce intermediates of alternative bile acid biosynthetic pathways. J. Biol. Chem. 273 (1998) 18153-18160. [PMID: 9660774]
8. Furster, C., Bergman, T. and Wikvall, K. Biochemical characterization of a truncated form of CYP27A purified from rabbit liver mitochondria. Biochem. Biophys. Res. Commun. 263 (1999) 663-666. [PMID: 10512735]
9. Pikuleva, I.A., Puchkaev, A. and Björkhem, I. Putative helix F contributes to regioselectivity of hydroxylation in mitochondrial cytochrome P450 27A1. Biochemistry 40 (2001) 7621-7629. [PMID: 11412116]
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]
Accepted name: cholesterol 7α-monooxygenase
Reaction: cholesterol + NADPH + H+ + O2 = 7α-hydroxycholesterol + NADP+ + H2O
For diagram click here.
Other name(s): cholesterol 7α-hydroxylase; CYP7A1
Systematic name: cholesterol,NADPH:oxygen oxidoreductase (7α-hydroxylating)
Comments: A heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9037-53-0
References:
1. Boyd, G.S., Grimwade, A.M. and Lawson, M.E. Studies on rat-liver microsomal cholesterol 7α-hydroxylase. Eur. J. Biochem. 37 (1973) 334-340. [PMID: 4147676]
2. Mitton, J.R., Scholan, N.A. and Boyd, G.S. The oxidation of cholesterol in rat liver sub-cellular particles. The cholesterol-7α-hydroxylase enzyme system. Eur. J. Biochem. 20 (1971) 569-579. [PMID: 4397276]
3. Ogishima, T., Deguchi, S. and Okuda, K. Purification and characterization of cholesterol 7α-hydroxylase from rat liver microsomes. J. Biol. Chem. 262 (1987) 7646-7650. [PMID: 3584134]
Accepted name: 4-hydroxyphenylacetate 1-monooxygenase
Reaction: 4-hydroxyphenylacetate + NAD(P)H + H+ + O2 = homogentisate + NAD(P)+ + H2O
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, EXPASY, KEGG, Metacyc, UM-BBD, 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, EXPASY, KEGG, Metacyc, UM-BBD, 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]
Accepted name: flavonoid 3'-monooxygenase
Reaction: a flavonoid + NADPH + H+ + O2 = a 3'-hydroxyflavonoid + NADP+ + H2O
See diagram for reaction in taxifolin or eriodictyol biosynthesis.
Other name(s): flavonoid 3'-hydroxylase; flavonoid 3-hydroxylase (erroneous); NADPH:flavonoid-3'-hydroxylase; flavonoid 3-monooxygenase (erroneous)
Systematic name: flavonoid,NADPH:oxygen oxidoreductase (3'-hydroxylating)
Comments: Acts on a number of flavonoids, including naringenin and dihydrokaempferol. Does not act on 4-coumarate or 4-coumaroyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 75991-44-5
References:
1. Forkmann, G., Heller, W. and Grisebach, H. Anthocyanin biosynthesis in flowers of Matthiola incana flavanone 3- and flavonoid 3'-hydroxylases. Z. Naturforsch. C: Biosci. 35 (1980) 691-695.
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, EXPASY, KEGG, Metacyc, UM-BBD, 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, EXPASY, KEGG, Metacyc, UM-BBD, 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, EXPASY, KEGG, Metacyc, UM-BBD, 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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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]
Accepted name: phosphatidylcholine 12-monooxygenase
Reaction: 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NADH + H+ + O2 = 1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + NAD+ + H2O
Other name(s): ricinoleic acid synthase; oleate δ12-hydroxylase; oleate δ12-monooxygenase
Systematic name: 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine,NADH:oxygen oxidoreductase (12-hydroxylating)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 77950-95-9
References:
1. Galliard, T. and Stumpf, P.K. Fat metabolism in higher plants. 30. Enzymatic synthesis of ricinoleic acid by a microsomal preparation from developing Ricinus communis seeds. J. Biol. Chem. 241 (1966) 5806-5812. [PMID: 4289003]
2. Moreau, R.A. and Stumpf, P.K. Recent studies of the enzymic-synthesis of ricinoleic acid by developing castor beans. Plant Physiol. 67 (1981) 672-676.
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, EXPASY, KEGG, Metacyc, UM-BBD, 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]
Accepted name: 3,9-dihydroxypterocarpan 6a-monooxygenase
Reaction: (6aR,11aR)-3,9-dihydroxypterocarpan + NADPH + H+ + O2 = (6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADP+ + H2O
For diagram click here.
Other name(s): 3,9-dihydroxypterocarpan 6a-hydroxylase; 3,9-dihydroxypterocarpan 6α-monooxygenase (erroneous)
Systematic name: (6aR,11aR)-3,9-dihydroxypterocarpan,NADPH:oxygen oxidoreductase (6a-hydroxylating)
Comments: Possibly a heme-thiolate protein (P-450). The product of the reaction is the biosynthetic precursor of the phytoalexin glyceollin in soybean.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 92584-16-2
References:
1. Hagmann, M.-L., Heller, W. and Grisebach, H. Induction of phytoalexin synthesis in soybean. Stereospecific 3,9-dihydroxypterocarpan 6a-hydroxylase from elicitor-induced soybean cell cultures.Eur. J. Biochem. 142 (1984) 127-131. [PMID: 6540173]
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, EXPASY, KEGG, Metacyc, UM-BBD, 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]
Accepted name: leukotriene-B4 20-monooxygenase
Reaction: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + NADPH + H+ + O2 = (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + NADP+ + H2O
Other name(s): leukotriene-B4 20-hydroxylase; leucotriene-B4 ω-hydroxylase; LTB4 20-hydroxylase; LTB4 ω-hydroxylase
Systematic name: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate,NADPH:oxygen oxidoreductase (20-hydroxylating)
Comments: A heme-thiolate protein (P-450). Not identical with EC 1.14.13.34, leukotriene-E4 20-monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 90119-11-2
References:
1. Romano, M.C., Eckardt, R.D., Bender, P.E., Leonard, T.B., Straub, K.M. and Newton, J.F. Biochemical characterization of hepatic microsomal leukotriene B4 hydroxylases. J. Biol. Chem. 262 (1987) 1590-1595. [PMID: 3027095]
2. Shak, S. and Goldstein, I.M. Leukotriene B4 ω-hydroxylase in human polymorphonuclear leukocytes. Partial purification and identification as a cytochrome P-450. J. Clin. Invest. 76 (1985) 1218-1228. [PMID: 4044832]
3. Soberman, R.J., Harper, T.W., Murphy, R.C. and Austen, K.F. Identification and functional characterization of leukotriene B4 20-hydroxylase of human polymorphonuclear leukocytes. Proc. Natl. Acad. Sci. USA 82 (1985) 2292-2295. [PMID: 2986111]
Accepted name: 2-nitrophenol 2-monooxygenase
Reaction: 2-nitrophenol + NADPH + H+ + O2 = catechol + nitrite + NADP+ + H2O
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, EXPASY, KEGG, Metacyc, UM-BBD, 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
Other name(s): albendazole oxidase; albendazole sulfoxidase
Systematic name: albendazole,NADPH:oxygen oxidoreductase (sulfoxide-forming)
Comments: A flavoprotein (FAD).
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]
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, 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, EXPASY, KEGG, Metacyc, UM-BBD, 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]
Accepted name: 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase
Reaction: trans-5-O-(4-coumaroyl)-D-quinate + NADPH + H+ + O2 = trans-5-O-caffeoyl-D-quinate + NADP+ + H2O
Other name(s): 5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase; coumaroylquinate(coumaroylshikimate) 3'-monooxygenase
Systematic name: trans-5-O-(4-coumaroyl)-D-quinate,NADPH:oxygen oxidoreductase (3'-hydroxylating)
Comments: Also acts on trans-5-O-(4-coumaroyl)shikimate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 112131-08-5
References:
1. Kühnl, T., Koch, U., Heller, W. and Wellman, E. Chlorogenic acid biosynthesis: characterization of a light-induced microsomal 5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase from carrot (Daucus carota L.) cell suspension cultures. Arch. Biochem. Biophys. 258 (1987) 226-232. [PMID: 2821918]
Accepted name: methyltetrahydroprotoberberine 14-monooxygenase
Reaction: (S)-N-methylcanadine + NADPH + H+ + O2 = allocryptopine + NADP+ + H2O
For diagram click here or here.
Other name(s): methyltetrahydroprotoberberine 14-hydroxylase; (S)-cis-N-methyltetrahydroberberine 14-monooxygenase; (S)-cis-N-methyltetrahydroprotoberberine-14-hydroxylase
Systematic name: (S)-N-methylcanadine,NADPH:oxygen oxidoreductase (14-hydroxylating)
Comments: A heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 113478-42-5
References:
1. Rueffer, M. and Zenk, M.H. Enzymatic formation of protopines by a microsomal cytochrome-P-450 system of Corydalis vaginans. Tetrahedron Lett. 28 (1987) 5307-5310.
Accepted name: anhydrotetracycline monooxygenase
Reaction: anhydrotetracycline + NADPH + H+ + O2 = 12-dehydrotetracycline + NADP+ + H2O
Other name(s): ATC oxygenase; anhydrotetracycline oxygenase
Systematic name: anhydrotetracycline,NADPH:oxygen oxidoreductase (6-hydroxylating)
Comments: Involved in the biosynthesis of the antibiotics tetracyclines in Streptomyces sp.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 70766-62-0
References:
1. Behal, V. The tetracycline fermentation and its regulation. CRC Crit. Rev. Biotechnol. 5 (1987) 295-318.
Accepted name: nitric-oxide synthase (NADPH dependent)
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
Other name(s): nitric oxide synthetase; endothelium-derived relaxation factor-forming enzyme; endothelium-derived relaxing factor synthase; NO synthase; NADPH-diaphorase
Systematic name: L-arginine,NADPH:oxygen oxidoreductase (nitric-oxide-forming)
Comments: Binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin. This eukaryotic enzyme, which is found in plants [4] and animals [1-3], consists of oxygenase and reductase domains that 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. May produce superoxide under certain conditions [3]. cf. EC 1.14.13.165, nitric-oxide synthase [NAD(P)H dependent].
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. 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: 2-aminobenzoyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
Other name(s): anthraniloyl coenzyme A reductase; 2-aminobenzoyl-CoA monooxygenase/reductase
Systematic name: 2-aminobenzoyl-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, EXPASY, KEGG, Metacyc, UM-BBD, 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]
Accepted name: tyrosine N-monooxygenase
Reaction: L-tyrosine + 2 O2 + 2 NADPH + 2 H+ = (Z)-[4-hydroxyphenylacetaldehyde oxime] + 2 NADP+ + CO2 + 3 H2O (overall reaction)
(1a) L-tyrosine + O2 + NADPH + H+ = N-hydroxy-L-tyrosine + NADP+ + H2O
(1b) N-hydroxy-L-tyrosine + O2 + NADPH + H+ = N,N-dihydroxy-L-tyrosine + NADP+ + H2O
(1c) N,N-dihydroxy-L-tyrosine = (Z)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
For diagram click here.
Other name(s): tyrosine N-hydroxylase; CYP79A1
Systematic name: L-tyrosine,NADPH:oxygen oxidoreductase (N-hydroxylating)
Comments: A heme-thiolate protein (P-450). This enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along with EC 1.14.13.68, 4-hydroxyphenylacetaldehyde oxime monooxygenase and EC 2.4.1.85, cyanohydrin β-glucosyltransferase. Some 2-(4-hydroxyphenyl)-1-nitroethane is formed as a side product.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 159447-19-5
References:
1. Halkier, B.A. and Møller, B.L. The biosynthesis of cyanogenic glucosides in higher plants. Identification of three hydroxylation steps in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench and the involvement of 1-ACI-nitro-2-(p-hydroxyphenyl)ethane as an intermediate. J. Biol. Chem. 265 (1990) 21114-21121. [PMID: 2250015]
2. Sibbesen, O., Koch, B., Halkier, B.A. and Møller, B.L. Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. J. Biol. Chem. 270 (1995) 3506-3511. [PMID: 7876084]
3. Bak, S., Olsen, C.E., Halkier, B.A. and Møller, B.L. Transgenic tobacco and Arabidopsis plants expressing the two multifunctional sorghum cytochrome P450 enzymes, CYP79A1 and CYP71E1, are cyanogenic and accumulate metabolites derived from intermediates in dhurrin biosynthesis. Plant Physiol. 123 (2000) 1437-1448. [PMID: 10938360]
4. Nielsen, J.S. and Møller, B.L. Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima. Plant Physiol. 122 (2000) 1311-1321. [PMID: 10759528]
5. Busk, P.K. and Møller, B.L. Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants. Plant Physiol. 129 (2002) 1222-1231. [PMID: 12114576]
6. Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and Bak, S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779-1784. [PMID: 15665094]
[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, EXPASY, KEGG, Metacyc, UM-BBD, 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]
Accepted name: (S)-limonene 3-monooxygenase
Reaction: (S)-limonene + NADPH + H+ + O2 = trans-isopiperitenol + NADP+ + H2O
For diagram click here.
Glossary:
limonene: a monoterpenoid
(S)-limonene = (–)-limonene
Other name(s): (–)-limonene 3-hydroxylase; (–)-limonene 3-monooxygenase; (–)-limonene,NADPH:oxygen oxidoreductase (3-hydroxylating)
Systematic name: (S)-limonene,NADPH:oxygen oxidoreductase (3-hydroxylating)
Comments: High specificity, but NADH can act instead of NADPH, although more slowly. A heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 138066-92-9
References:
1. Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (–)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219-226. [PMID: 2297225]
Accepted name: (S)-limonene 6-monooxygenase
Reaction: (S)-limonene + NADPH + H+ + O2 = trans-carveol + NADP+ + H2O
For diagram click here.
Glossary:
limonene: a monoterpenoid
(S)-limonene = (–)-limonene
Other name(s): (–)-limonene 6-hydroxylase; (–)-limonene 6-monooxygenase; (–)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating)
Systematic name: (S)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating)
Comments: High specificity, but NADH can act instead of NADPH, but more slowly. A heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 138066-93-0
References:
1. Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (–)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219-226. [PMID: 90120595]
Accepted name: (S)-limonene 7-monooxygenase
Reaction: (S)-limonene + NADPH + H+ + O2 = (–)-perillyl alcohol + NADP+ + H2O
For diagram click here.
Glossary:
limonene: a monoterpenoid
(S)-limonene = (–)-limonene
Other name(s): (–)-limonene 7-monooxygenase; (–)-limonene hydroxylase; (–)-limonene monooxygenase; (–)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating)
Systematic name: (S)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating)
Comments: High specificity, but NADH can act instead of NADPH, although more slowly. A heme-thiolate protein (P-450).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 122653-75-2
References:
1. Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (–)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219-226. [PMID: 2297225]
Accepted name: pentachlorophenol monooxygenase
Reaction: (1) pentachlorophenol + 2 NADPH + H+ + O2 = 2,3,5,6-tetrachlorohydroquinone + 2 NADP+ + chloride + H2O
(2) 2,3,5,6-tetrachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachlorohydroquinone + NADP+ + H2O
Other name(s): pentachlorophenol dechlorinase; pentachlorophenol dehalogenase; pentachlorophenol 4-monooxygenase; PCP hydroxylase; pentachlorophenol hydroxylase; PcpB; 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]. The enzyme converts many polyhalogenated phenols into hydroquinones, and requires that a halogen substituent be present at C-2 [2]. If C-4 carries a halogen substituent, reaction 1 is catalysed, e.g. 2,4,6-triiodophenol is oxidized to 2,6-diiodohydroquinone; if C-4 is unsubstituted, reaction 2 is catalysed.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, 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]