Information on EC 1.4.3.23 - 7-chloro-L-tryptophan oxidase

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The expected taxonomic range for this enzyme is: Lechevalieria aerocolonigenes

EC NUMBER
COMMENTARY hide
1.4.3.23
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RECOMMENDED NAME
GeneOntology No.
7-chloro-L-tryptophan oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7-chloro-L-tryptophan + O2 = 2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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K-252 biosynthesis
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rebeccamycin biosynthesis
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staurosporine biosynthesis
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Staurosporine biosynthesis
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violacein biosynthesis
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
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?
5-fluoro-L-tryptophan + O2
?
show the reaction diagram
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?
5-methyl-DL-tryptophan + O2
?
show the reaction diagram
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?
7-chloro-L-tryptophan + O2
2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2
show the reaction diagram
additional information
?
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L-tryptophanamide and N-acetyl-tryptophan are not accepted as substrates by RebO
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q8KHS0
rebeccamycin biosynthetic pathway
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?
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, 30C
1.84
5-fluoro-L-tryptophan
pH 7.8, 30C
0.088
7-chloro-L-tryptophan
pH 7.8, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0255
1-methyl-L-tryptophan
Lechevalieria aerocolonigenes
Q8KHS0
pH 7.8, 30C
0.239
5-fluoro-L-tryptophan
Lechevalieria aerocolonigenes
Q8KHS0
pH 7.8, 30C
0.664
7-chloro-L-tryptophan
Lechevalieria aerocolonigenes
Q8KHS0
pH 7.8, 30C
0.202
L-Trp
Lechevalieria aerocolonigenes
Q8KHS0
pH 7.8, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0178
1-methyl-L-tryptophan
Lechevalieria aerocolonigenes
Q8KHS0
pH 7.8, 30C
2254
0.13
5-fluoro-L-tryptophan
Lechevalieria aerocolonigenes
Q8KHS0
pH 7.8, 30C
9768
7.55
7-chloro-L-tryptophan
Lechevalieria aerocolonigenes
Q8KHS0
pH 7.8, 30C
11727
0.132
L-Trp
Lechevalieria aerocolonigenes
Q8KHS0
pH 7.8, 30C
420
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53412
2 * 53412, calculated from sequence
56000
x * 56000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 53412, calculated from sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of N-His6-tagged RebO in Escherichia coli