| EC |
1.14.13.7 |
| Accepted name: |
phenol 2-monooxygenase (NADPH) |
| Reaction: |
phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O |
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For diagram of catechol biosynthesis, 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, Gene, 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 810352] |
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| [EC 1.14.13.7 created 1972, modified 2011, modified 2016] |
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