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

for references in articles please use BRENDA:EC1.14.99.52
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The enzyme appears in viruses and cellular organisms

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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A0A1D8U0C7, A0A1D8U386
UniProt
Manually annotated by BRENDA team
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A0A1D8U0C7, A0A1D8U386
UniProt
Manually annotated by BRENDA team
collected in the Gulf of Naples, near Castel dell'Ovo, from a location that is not privately-owned or protected in any way, and in collected at the Marine Protected Area Gaiola at station G1 in October of 2013
UniProt
Manually annotated by BRENDA team
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-
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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 + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-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
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-
-
?
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
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-
-
?
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 + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-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
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
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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
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pH 8.0, 26°C
0.23
histamine
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pH 8.0, 26°C
0.35
L-cysteine
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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
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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
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pH 8.0, 26°C
0.36
histamine
-
pH 8.0, 26°C
3.3
L-cysteine
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pH 8.0, 26°C, with L-histidine
0.57
L-histidinamide
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pH 8.0, 26°C
3.4
L-histidine
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pH 8.0, 26°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
4-methylimidazole
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pH 8.0, 26°C
1.2
D-histidine
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pH 8.0, 26°C
1.6
histamine
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pH 8.0, 26°C
9.43
L-cysteine
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pH 8.0, 26°C, with L-histidine
1.8
L-histidinamide
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pH 8.0, 26°C
10
L-histidine
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pH 8.0, 26°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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, multi-exonic gene with 18 exons, DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis
gene ovoA, multi-exonic gene with 19 exons, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real time PCR enzyme expression analysis
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
at the pluteus stage PlOvoA mRNA is strongly downregulated after exposure to 0.005-0.010 mM Cd2+
PlOvoA embryo expression significantly increases at the pluteus stage and is upregulated by metals (Cd2+ and Mn2+) at concentrations mimicking polluted sea-water and by cyclic toxic algal blooms, leading to ovothiol biosynthesis. In silico analysis of the PlOvoA upstream region reveals metal and stress responsive elements. PlOvoA expression profile and response to environmental stress conditions, overview. A significant increase of PlOvoA mRNA is observed at the swimming blastula stage after exposure to 0.001-0.005 mM Cd2+, whereas at the early blastula and prism stages, the gene transcription is unaffected. On the contrary, at the pluteus stage PlOvoA mRNA is strongly down-regulated after exposure to 0.005-0.010 mM Cd2+. In the presence of Mn2+, the relative expression ratio of PlOvoA at the swimming blastula stage is close to the minimum value considered significant. No appreciable gene regulation is observed in other developmental stages
SpOvoA upstream region analysis reveals several metal and stress responsive elements, overview
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
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