Entry |
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Name |
7-chloro-L-tryptophan oxidase;
RebO
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Class |
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With oxygen as acceptor
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Sysname |
7-chloro-L-tryptophan:oxygen oxidoreductase
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Reaction(IUBMB) |
7-chloro-L-tryptophan + O2 = 2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2 [RN: R09560]
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Reaction(KEGG) |
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Substrate |
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Product |
2-imino-3-(7-chloroindol-3-yl)propanoate [CPD: C19688];
H2O2 [CPD: C00027]
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Comment |
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].
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History |
EC 1.4.3.23 created 2010
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Pathway |
ec01110 | Biosynthesis of secondary metabolites |
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Orthology |
K19884 | 7-chloro-L-tryptophan oxidase |
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Reference |
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Authors |
Nishizawa T, Aldrich CC, Sherman DH |
Title |
Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243. |
Journal |
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Sequence |
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Reference |
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Authors |
Howard-Jones AR, Walsh CT |
Title |
Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD. |
Journal |
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Sequence |
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Other DBs |
ExplorEnz - The Enzyme Database: | 1.4.3.23 |
ExPASy - ENZYME nomenclature database: | 1.4.3.23 |
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