| EC |
1.4.3.23 |
| Accepted name: |
7-chloro-L-tryptophan oxidase |
| Reaction: |
7-chloro-L-tryptophan + O2 = 2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2 |
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For diagram of rebeccamycin biosynthesis, click here |
| Other name(s): |
RebO |
| Systematic name: |
7-chloro-L-tryptophan:oxygen oxidoreductase |
| Comments: |
Contains a noncovalently bound FAD [1,2]. This enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. During catalysis, the bound FAD is reoxidized at the expense of molecular oxygen, producing one molecule of hydrogen peroxide. The enzyme shows significant preference for 7-chloro-L-tryptophan over L-tryptophan [1]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Nishizawa, T., Aldrich, C.C. and Sherman, D.H. Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243. J. Bacteriol. 187 (2005) 2084–2092. [DOI] [PMID: 15743957] |
| 2. |
Howard-Jones, A.R. and Walsh, C.T. Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD. Biochemistry 44 (2005) 15652–15663. [DOI] [PMID: 16313168] |
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| [EC 1.4.3.23 created 2010] |
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