| EC |
1.14.13.84 |
| Accepted name: |
4-hydroxyacetophenone monooxygenase |
| Reaction: |
(4-hydroxyphenyl)ethan-1-one + NADPH + H+ + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O |
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For diagram of reaction, click here |
| Other name(s): |
HAPMO |
| Systematic name: |
(4-hydroxyphenyl)ethan-1-one,NADPH:oxygen oxidoreductase (ester-forming) |
| Comments: |
Contains FAD. The enzyme from Pseudomonas fluorescens ACB catalyses the conversion of a wide range of acetophenone derivatives. Highest activity occurs with compounds bearing an electron-donating substituent at the para position of the aromatic ring [1]. In the absence of substrate, the enzyme can act as an NAD(P)H oxidase (EC 1.6.3.1). |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 156621-13-5 |
| References: |
| 1. |
Kamerbeek, N.M., Moonen, M.J., van der Ven, J.G., van Berkel, W.J.H., Fraaije, M.W. and Janssen, D.B. 4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB: a novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds. Eur. J. Biochem. 268 (2001) 2547–2557. [DOI] [PMID: 11322873] |
| 2. |
Kamerbeek, N.M, Olsthoorn, A.J.J., Fraaije, M.W. and Janssen, D.B. Substrate specificity of a novel Baeyer-Villiger monooxygenase, 4-hydroxyacetophenone monooxygenase. Appl. Environ. Microbiol. 69 (2003) 419–426. [DOI] [PMID: 12514023] |
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| [EC 1.14.13.84 created 2004] |
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