KEGG   ORTHOLOGY: K19884Help
Entry
K19884                      KO                                     

Name
rebO
Definition
7-chloro-L-tryptophan oxidase [EC:1.4.3.23]
Pathway
ko00404  Staurosporine biosynthesis
ko01100  Metabolic pathways
ko01130  Biosynthesis of antibiotics
Module
M00789  Rebeccamycin biosynthesis, tryptophan => rebeccamycin
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09110 Biosynthesis of other secondary metabolites
   00404 Staurosporine biosynthesis
    K19884  rebO; 7-chloro-L-tryptophan oxidase
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.4  Acting on the CH-NH2 group of donors
   1.4.3  With oxygen as acceptor
    1.4.3.23  7-chloro-L-tryptophan oxidase
     K19884  rebO; 7-chloro-L-tryptophan oxidase
BRITE hierarchy
Other DBs
RN: R09560
COG: COG1231
Genes
AG: BAC10674(rebO)
TaxonomyKoalaUniProt
Reference
  Authors
Nishizawa T, Aldrich CC, Sherman DH
  Title
Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243.
  Journal
J Bacteriol 187:2084-92 (2005)
DOI:10.1128/JB.187.6.2084-2092.2005
  Sequence
Reference
  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
Biochemistry 44:15652-63 (2005)
DOI:10.1021/bi051706e

KEGG   ENZYME: 1.4.3.23Help
Entry
EC 1.4.3.23                 Enzyme                                 

Name
7-chloro-L-tryptophan oxidase;
RebO
Class
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
7-chloro-L-tryptophan:oxygen oxidoreductase
Reaction(IUBMB)
7-chloro-L-tryptophan + O2 = 2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2 [RN:R09560]
Reaction(KEGG)
Substrate
7-chloro-L-tryptophan [CPD:C19687];
O2 [CPD:C00007]
Product
2-imino-3-(7-chloroindol-3-yl)propanoate [CPD:C19688];
H2O2 [CPD:C00027]
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].
History
EC 1.4.3.23 created 2010
Pathway
ec00404  Staurosporine biosynthesis
ec01100  Metabolic pathways
ec01130  Biosynthesis of antibiotics
Orthology
K19884  7-chloro-L-tryptophan oxidase
Reference
1  [PMID:15743957]
  Authors
Nishizawa T, Aldrich CC, Sherman DH
  Title
Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243.
  Journal
J Bacteriol 187:2084-92 (2005)
DOI:10.1128/JB.187.6.2084-2092.2005
  Sequence
Reference
2  [PMID:16313168]
  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
Biochemistry 44:15652-63 (2005)
DOI:10.1021/bi051706e
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.4.3.23
IUBMB Enzyme Nomenclature: 1.4.3.23
ExPASy - ENZYME nomenclature database: 1.4.3.23
BRENDA, the Enzyme Database: 1.4.3.23

KEGG   REACTION: R09560Help
Entry
R09560                      Reaction                               

Name
7-chloro-L-tryptophan:oxygen oxidoreductase
Definition
7-Chloro-L-tryptophan + Oxygen <=> 2-Imino-3-(7-chloroindol-3-yl)propanoate + Hydrogen peroxide
Equation
Reaction class
RC02566  C19687_C19688
RC02755  C00007_C00027
Enzyme
Pathway
rn00404  Staurosporine biosynthesis
rn01100  Metabolic pathways
rn01130  Biosynthesis of antibiotics
Module
M00789  Rebeccamycin biosynthesis, tryptophan => rebeccamycin
Orthology
K19884  7-chloro-L-tryptophan oxidase [EC:1.4.3.23]
Other DBs
RHEA: 27305

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