Information on EC 1.14.19.B7 - tryptophan 5-halogenase

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The expected taxonomic range for this enzyme is: Streptomyces rugosporus

EC NUMBER
COMMENTARY hide
1.14.19.B7
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
tryptophan 5-halogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + FADH2 + Cl- + O2 + H+ = 5-chloro-L-tryptophan + FAD + 2 H2O
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
halogenation
-
-
SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:FADH2 oxidoreductase (5-halogenating)
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-tryptophan + FADH2 + Br- + O2 + H+
5-bromo-L-tryptophan + FAD + 2 H2O
show the reaction diagram
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
show the reaction diagram
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
L-tryptophan + FADH2 + Br- + O2 + H+
5-bromo-L-tryptophan + FAD + 2 H2O
show the reaction diagram
-
-
-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
5-chloro-L-tryptophan + FAD + 2 H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-tryptophan
-
substrate inhibition above 0.06 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.071 - 0.15
L-tryptophan
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00813
L-tryptophan
Streptomyces rugosporus
-
pH 7.2, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0542
L-tryptophan
Streptomyces rugosporus
-
pH 7.2, 30°C
119
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
half-life 1848 min
30
-
half-life 43 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using a nickel-chelating HisTrap HP column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
for expression in Pseudomonas fluorescens
-
His-tagged apoPyrH was expressed in Pseudomonas fluorescens BL915
-
overexpression in Pseudomonas fluorescens BL915 DELTAORF1
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E46D
-
mutant enzyme folds properly
E46Q
-
mutant enzyme folds properly
F49A/Y454F
-
mutant enzyme is incorrectly folded
E46D
-
mutant enzyme folds properly
-
E46Q
-
mutant enzyme folds properly
-
F49A/Y454F
-
mutant enzyme is incorrectly folded
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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