Information on EC 1.14.99.52 - L-cysteinyl-L-histidinylsulfoxide synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.14.99.52
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RECOMMENDED NAME
GeneOntology No.
L-cysteinyl-L-histidinylsulfoxide synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
L-histidine,L-cysteine:oxygen [S-(L-histidin-5-yl)-L-cysteine S-oxide-forming]
Requires Fe2+ for activity. The enzyme participates in ovothiol biosynthesis. It also has some activity as EC 1.13.11.20, cysteine dioxygenase, and can perform the reaction of EC 1.14.99.50, gamma-glutamyl hercynylcysteine sulfoxide synthase, albeit with low activity [4].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-fluoro-L-histidine + L-cysteine + O2
S-(2-fluoro-L-histidin-5-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
4-methylimidazole + L-cysteine + O2
? + H2O
show the reaction diagram
D-histidine + L-cysteine + O2
S-(D-histidin-5-yl)-L-cysteine S-oxide + S-(D-histidin-2-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
histamine + L-cysteine + O2
S-(histamin-5-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
-
-
-
?
L-cysteine + O2
cysteine sulfinic acid + H2O
show the reaction diagram
L-cysteine + O2
L-cystine + H2O
show the reaction diagram
L-histidinamide + L-cysteine + O2
S-(L-histidinamide-5-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
-
-
-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
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
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
-
provides a nearly 100fold increase in enzyme activity
D-isoascorbate
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provides a nearly 100fold increase in enzyme activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.67
D-histidine
-
pH 8.0, 26°C
0.23
histamine
-
pH 8.0, 26°C
0.35
L-cysteine
-
pH 8.0, 26°C, with L-histidine
0.31
L-histidinamide
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pH 8.0, 26°C
0.34
L-histidine
-
pH 8.0, 26°C
additional information
additional information
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free-energy cost calculations for determining the catalytic mechanism, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.78
D-histidine
Erwinia tasmaniensis
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pH 8.0, 26°C
0.36
histamine
Erwinia tasmaniensis
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pH 8.0, 26°C
3.3
L-cysteine
Erwinia tasmaniensis
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pH 8.0, 26°C, with L-histidine
0.57
L-histidinamide
Erwinia tasmaniensis
-
pH 8.0, 26°C
3.4
L-histidine
Erwinia tasmaniensis
-
pH 8.0, 26°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
4-methylimidazole
Erwinia tasmaniensis
-
pH 8.0, 26°C
16907
1.2
D-histidine
Erwinia tasmaniensis
-
pH 8.0, 26°C
3068
1.6
histamine
Erwinia tasmaniensis
-
pH 8.0, 26°C
605
9.43
L-cysteine
Erwinia tasmaniensis
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pH 8.0, 26°C, with L-histidine
74
1.8
L-histidinamide
Erwinia tasmaniensis
-
pH 8.0, 26°C
56975
10
L-histidine
Erwinia tasmaniensis
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pH 8.0, 26°C
349
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant Strep-tagged enzyme from Escherichia coli by affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene ovoA, recombinant expression of His-tagged enzyme in Escherichia coli
gene ovoA, the mutant enzyme loses the cysteine dioxygenase activity but also stops catalyzing the formation of oxidative coupling product
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recombinant overexpression of Strep-tagged enzyme in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E176A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
E176H
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site-directed mutagenesis
H170A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
H174A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
E176A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
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E176H
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site-directed mutagenesis
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H170A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
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H174A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis