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Information on EC 1.4.3.23 - 7-chloro-L-tryptophan oxidase and Organism(s) Lentzea aerocolonigenes and UniProt Accession Q8KHS0

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IUBMB 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 .
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Lentzea aerocolonigenes
UNIPROT: Q8KHS0
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The taxonomic range for the selected organisms is: Lentzea aerocolonigenes
The enzyme appears in selected viruses and cellular organisms
Synonyms
RebO, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
7-chloro-L-tryptophan:oxygen oxidoreductase
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-methyl-L-tryptophan + O2
?
show the reaction diagram
-
-
-
?
5-fluoro-L-tryptophan + O2
?
show the reaction diagram
-
-
-
?
5-methyl-DL-tryptophan + O2
?
show the reaction diagram
-
-
-
?
7-chloro-L-tryptophan + O2
2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2
show the reaction diagram
L-Trp + O2
?
show the reaction diagram
-
-
-
?
7-chloro-L-tryptophan + O2
2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
2-imino-3-(indol-3-yl)propanoate + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
L-tryptophanamide and N-acetyl-tryptophan are not accepted as substrates by RebO
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
7-chloro-L-tryptophan + O2
2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2
show the reaction diagram
rebeccamycin biosynthetic pathway
-
-
?
7-chloro-L-tryptophan + O2
2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2
show the reaction diagram
-
-
-
-
?
L-tryptophan + O2
2-imino-3-(indol-3-yl)propanoate + H2O2
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.43
1-methyl-L-tryptophan
pH 7.8, 30°C
1.84
5-fluoro-L-tryptophan
pH 7.8, 30°C
0.088
7-chloro-L-tryptophan
pH 7.8, 30°C
1.53
L-Trp
pH 7.8, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0255
1-methyl-L-tryptophan
pH 7.8, 30°C
0.239
5-fluoro-L-tryptophan
pH 7.8, 30°C
0.664
7-chloro-L-tryptophan
pH 7.8, 30°C
0.202
L-Trp
pH 7.8, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0178
1-methyl-L-tryptophan
pH 7.8, 30°C
0.13
5-fluoro-L-tryptophan
pH 7.8, 30°C
7.55
7-chloro-L-tryptophan
pH 7.8, 30°C
0.132
L-Trp
pH 7.8, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
REBO_LENAE
473
0
51897
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
gel filtration
53412
2 * 53412, calculated from sequence
56000
x * 56000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 56000, SDS-PAGE
dimer
2 * 53412, calculated from sequence
?
-
x * 56000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of N-His6-tagged RebO in Escherichia coli
expressed in Escherichia coli C41 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Howard-Jones, A.R.; Walsh, C.T.
Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD
Biochemistry
44
15652-15663
2005
Lentzea aerocolonigenes (Q8KHS0)
Manually annotated by BRENDA team
Nishizawa, T.; Aldrich, C.C.; Sherman, D.H.
Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243
J. Bacteriol.
187
2084-2092
2005
Lentzea aerocolonigenes (Q8KHS0)
Manually annotated by BRENDA team
Spolitak, T.; Ballou, D.P.
Evidence for catalytic intermediates involved in generating the chromopyrrolic acid scaffold of rebeccamycin by RebO and RebD
Arch. Biochem. Biophys.
573
111-119
2015
Lentzea aerocolonigenes
Manually annotated by BRENDA team