1.14.19.58: tryptophan 5-halogenase
This is an abbreviated version!
For detailed information about tryptophan 5-halogenase, go to the full flat file.
Word Map on EC 1.14.19.58
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1.14.19.58
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halogenases
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flavin-dependent
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regioselective
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7-halogenase
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chlorinate
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indole
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synthesis
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albogriseolus
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biocatalysts
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brominate
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cl
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flavin
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pharmacology
- 1.14.19.58
- halogenases
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flavin-dependent
-
regioselective
-
7-halogenase
-
chlorinate
- indole
- synthesis
- albogriseolus
-
biocatalysts
-
brominate
- cl
- flavin
- pharmacology
Reaction
Synonyms
halogenase, mibH, pyrH, sttH, trp-5-halogenase
ECTree
1.14.19.58 tryptophan 5-halogenaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.14.19.58 - tryptophan 5-halogenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-indolepropionate + FADH2 + chloride + O2 + H+
6-chloro-3-indolepropionate + 5-chloro-3-indolepropionate + FAD + 2 H2O
57% conversion by the wild-type enzyme, 75% 5-chlorination is by mutant L460F/P461E/P462T in comparison to 90% 6-chlorination by the wild-type SttH
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-
?
anthranilamide + FADH2 + chloride + O2 + H+
5-chloro-anthranilamide + FAD + 2 H2O
43% conversion by the wild-type enzyme
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-
?
anthranilate + FADH2 + chloride + O2 + H+
5-chloro-anthranilate + FAD + 2 H2O
1.1% conversion by the wild-type enzyme
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-
?
indole-3-acetic acid + FADH2 + chloride + O2 + H+
5-chloroindole-3-acetic acid + FAD + 2 H2O
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-
-
?
kynurenine + FADH2 + chloride + O2 + H+
5-chloro-kynurenine + FAD + 2 H2O
79% conversion by the wild-type enzyme
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-
?
lantibiotic NAI-107-[tryptophan] + FADH2 + Cl- + O2 + H+
lantibiotic NAI-107-[5-chlorotryptophan] + FAD + 2 H2O
N-phenylanthranilate + FADH2 + chloride + O2 + H+
5-chloro-N-phenylanthranilate + FAD + 2 H2O
20% conversion by the wild-type enzyme
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-
?
L-tryptophan + FADH2 + Br- + O2 + H+
5-bromo-L-tryptophan + FAD + 2 H2O
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-
-
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?
L-tryptophan + FADH2 + Br- + O2 + H+
5-bromo-L-tryptophan + FAD + 2 H2O
brominating activity is about 75% of the chlorinating activity
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-
?
L-tryptophan + FADH2 + Br- + O2 + H+
5-bromo-L-tryptophan + FAD + 2 H2O
brominating activity is about 75% of the chlorinating activity
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-
?
L-tryptophan + FADH2 + chloride + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
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-
-
?
L-tryptophan + FADH2 + chloride + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
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-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
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-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
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-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
-
-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
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-
-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
pyrroindomycin biosynthesis
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-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
the enzyme is involved in the biosynthesis of the antibiotic pyrroindomycin B that contains an indole ring chlorinated in the 5 position
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-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
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-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
the enzyme is involved in the biosynthesis of the antibiotic pyrroindomycin B that contains an indole ring chlorinated in the 5 position
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-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
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-
-
?
lantibiotic NAI-107-[tryptophan] + FADH2 + Cl- + O2 + H+
lantibiotic NAI-107-[5-chlorotryptophan] + FAD + 2 H2O
NAI-107 acts as a peptidoglycan biosynthesis inhibitor by sequestering the cell wall precursor lipid II
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-
?
lantibiotic NAI-107-[tryptophan] + FADH2 + Cl- + O2 + H+
lantibiotic NAI-107-[5-chlorotryptophan] + FAD + 2 H2O
NAI-107 acts as a peptidoglycan biosynthesis inhibitor by sequestering the cell wall precursor lipid II
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-
?
additional information
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structure-based analysis of the enzyme's substrate specificity, structure-function relationship, overview
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?
additional information
?
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structure-based analysis of the enzyme's substrate specificity, structure-function relationship, overview
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?
