Information on EC 1.14.19.9 - tryptophan 7-halogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.19.9
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RECOMMENDED NAME
GeneOntology No.
tryptophan 7-halogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-L-tryptophan + FAD + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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pyrrolnitrin biosynthesis
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rebeccamycin biosynthesis
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Staurosporine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:FADH2 oxidoreductase (7-halogenating)
In the bacterium Lechevalieria aerocolonigenes the enzyme catalyses the initial step in the biosynthesis of rebeccamycin [2]. Also acts on bromide ion.
CAS REGISTRY NUMBER
COMMENTARY hide
198575-11-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 39243. Halogenation requires the presence of RebF, which catalyzes the NADH-dependent reduction of FAD to provide FADH2 for the halogenase
SwissProt
Manually annotated by BRENDA team
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+
7-bromo-L-tryptophan + FAD + H2O
show the reaction diagram
L-tryptophan + FADH2 + Cl- + O2
7-chloro-L-tryptophan + FAD + H2O
show the reaction diagram
L-tryptophan + FADH2 + Cl- + O2 + H+
7-chloro-L-tryptophan + FAD + H2O
show the reaction diagram
tryptamine + FADH2 + Cl- + O2 + H+
7-chloro-L-tryptamine + FAD + H2O
show the reaction diagram
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-
-
-
?
tryptophan + FADH2 + Cl- + O2 + H+
7-chloro-L-tryptophan + FAD + 2 H2O
show the reaction diagram
-
-
-
-
?
tryptophan + FADH2 + Cl- + O2 + H+
7-chloro-L-tryptophan + FAD + H2O
show the reaction diagram
-
-
-
-
?
tryptophan + FADH2 + Cl- + O2 + H+
7-chloro-tryptophan + FAD + H2O
show the reaction diagram
tryptophan + FADH2 + O2 + Cl- + H+
7-chlorotryptophan + FAD + H2O
show the reaction diagram
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initial step of rebeccamycin biosynthesis
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?
additional information
?
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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
L-tryptophan + FADH2 + Cl- + O2
7-chloro-L-tryptophan + FAD + H2O
show the reaction diagram
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formation of 7-chlorotryptophan as the initial step in the biosynthesis of antitumor agent rebeccamycin
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-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
7-chloro-L-tryptophan + FAD + H2O
show the reaction diagram
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the enzyme is involved in biosynthesis of pyrrolnitrin
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?
tryptophan + FADH2 + Cl- + O2 + H+
7-chloro-L-tryptophan + FAD + 2 H2O
show the reaction diagram
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-
-
-
?
tryptophan + FADH2 + Cl- + O2 + H+
7-chloro-L-tryptophan + FAD + H2O
show the reaction diagram
-
-
-
-
?
tryptophan + FADH2 + Cl- + O2 + H+
7-chloro-tryptophan + FAD + H2O
show the reaction diagram
tryptophan + FADH2 + O2 + Cl- + H+
7-chlorotryptophan + FAD + H2O
show the reaction diagram
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initial step of rebeccamycin biosynthesis
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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dependent on, binding structure, overview
FADH2
flavin
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dependent on
additional information
no cofactor: NADPH, FMN
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
formate
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complete loss of activity above 200 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
L-tryptophan
pH 7.5
0.0499 - 1.814
tryptophan
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 0.12
FADH2
0.023
L-tryptophan
Lechevalieria aerocolonigenes
Q8KHZ8
pH 7.5
0.018 - 0.11
tryptophan
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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PrnA activities are determined after addition of flavin reductase (SsuE). Without reductase, fractions after elution from the molecular sieve column do not show any activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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end-point assay for single-turnover reactions
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61074
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x * 61074, native protein, x * 61641, selenomethionine derivative, mass spectrometry
61641
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x * 61074, native protein, x * 61641, selenomethionine derivative, mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 61074, native protein, x * 61641, selenomethionine derivative, mass spectrometry
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo-enzyme or enzyme bound to FAD or L-tryptophan, X-ray diffraction structure determination and analysis at 2.08-2.3 A resolution
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hanging drop method, structural analysis of RebH in its apo-form as well as in a complex with both tryptophan and FAD
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hanging drop method, structural analysis of the enzyme in its apo-form as well as in a complex with both tryptophan and FAD at resolution of 2.5 A
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in complex with tryptophan and FAD and selenomethionine derivative
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protein without ligands and in presence of tryptophan and 7-chlorotryptophan
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel chelating Sepharose column chromatography
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RebH is purified by size-exclusion chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned by PCR and fused to the tac promoter from Escherichia coli
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expressed in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli strain BL21(DE3)
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mutant enzyme Y455W is expressed in Catharanthus roseus
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K79A
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inactive mutant with abolished FAD binding
K79M
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inactive mutant with abolished FAD binding
Y455W
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the mutant preferentially uses tryptamine as substrate
F103A
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the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
F103A/W455A
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inactive
H101A
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the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
W455A
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the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
additional information
Show AA Sequence (101 entries)
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