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Enzyme Nomenclature
Information on EC 1.14.19.B7 - tryptophan 5-halogenase
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The expected taxonomic range for this enzyme is: Streptomyces rugosporus
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EC NUMBER 
COMMENTARY 
1.14.19.B7
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
tryptophan 5-halogenase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + FADH2 + Cl- + O2 + H+ = 5-chloro-L-tryptophan + FAD + 2 H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:FADH2 oxidoreductase (5-halogenating)
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
a gene disruption mutant in the tryptophan 5-halogenase gene no longer produces the pyrroindomycin B, but still produces pyrroindomycin A, the nonhalogenated derivative
malfunction
-
a gene disruption mutant in the tryptophan 5-halogenase gene no longer produces the pyrroindomycin B, but still produces pyrroindomycin A, the nonhalogenated derivative
-
physiological function
-
the enzyme is involved in the biosynthesis of the antibiotic pyrroindomycin B that contains an indole ring chlorinated in the 5 position
physiological function
-
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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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
L-tryptophan + FADH2 + Br- + O2 + H+
5-bromo-L-tryptophan + FAD + 2 H2O
-
-
-
-
?
L-tryptophan + FADH2 + Br- + O2 + H+
5-bromo-L-tryptophan + FAD + 2 H2O
brominating activity is about 75% of the chlorinating activity
-
-
?
L-tryptophan + FADH2 + Br- + O2 + H+
5-bromo-L-tryptophan + FAD + 2 H2O
brominating activity is about 75% of the chlorinating activity
-
-
?
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
-
-
-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
-
pyrroindomycin biosynthesis
-
-
?
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
-
-
?
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
-
-
-
?
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
L-tryptophan + FADH2 + Br- + O2 + H+
5-bromo-L-tryptophan + FAD + 2 H2O
-
-
-
-
?
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
-
pyrroindomycin biosynthesis
-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
A4D0H5
the enzyme is involved in the biosynthesis of the antibiotic pyrroindomycin B that contains an indole ring chlorinated in the 5 position
-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
A4D0H5
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor-diffusion method at 20°C, crystal structure of a tryptophan 5-halogenase (PyrH) bound to tryptophan and FAD
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
5-Br- and 5-Cl-tryptophan could presumably be applied as a pharmacologically attractive precursor of serotonin
synthesis
-
use of enzyme in selective halogenation of organic compounds
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.19.B7)
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