PMID:15743957

Nishizawa T, Aldrich CC, Sherman DH

Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243.

J Bacteriol 187:2084-92 (2005)
DOI:10.1128/JB.187.6.2084-2092.2005

[ag:BAC10674]

PMID:16313168

Howard-Jones AR, Walsh CT

Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD.

Biochemistry 44:15652-63 (2005)
DOI:10.1021/bi051706e

Oxidoreductases;
Acting on the CH-NH2 group of donors;
With oxygen as acceptor
BRITE hierarchy

7-chloro-L-tryptophan:oxygen oxidoreductase

7-chloro-L-tryptophan + O2 = 2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2 [RN:R09560]

R09560
Reaction

7-chloro-L-tryptophan [CPD:C19687];
O2 [CPD:C00007]

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].

EC 1.4.3.23 created 2010

1  [PMID:15743957]

Nishizawa T, Aldrich CC, Sherman DH

Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243.

J Bacteriol 187:2084-92 (2005)
DOI:10.1128/JB.187.6.2084-2092.2005

[ag:BAC10674]

2  [PMID:16313168]

Howard-Jones AR, Walsh CT

Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD.

Biochemistry 44:15652-63 (2005)
DOI:10.1021/bi051706e

[ag:BAC10674]