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show all sequences of 1.14.99.52

Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis

Song, H.; Her, A.S.; Raso, F.; Zhen, Z.; Huo, Y.; Liu, P.; Org. Lett. 16, 2122-2125 (2014)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
potential application of the oxidative coupling between hercynine and cysteine for industrial ergothioneine production
Erwinia tasmaniensis
Cloned(Commentary)
Commentary
Organism
gene ovoA, the mutant enzyme loses the cysteine dioxygenase activity but also stops catalyzing the formation of oxidative coupling product
Erwinia tasmaniensis
Engineering
Amino acid exchange
Commentary
Organism
E176H
site-directed mutagenesis
Erwinia tasmaniensis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
a mononuclear non-heme iron enzyme, dependent on, ligand with 2-His-1-carboxylate facial triad
Erwinia tasmaniensis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-histidine + L-cysteine + O2
Erwinia tasmaniensis
-
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
?
L-histidine + L-cysteine + O2
Erwinia tasmaniensis DSM 17950
-
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Erwinia tasmaniensis
B2VFD8
gene ovoA
-
Erwinia tasmaniensis DSM 17950
B2VFD8
gene ovoA
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hercynine + L-cysteine + O2
-
734828
Erwinia tasmaniensis
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
-
734828
Erwinia tasmaniensis DSM 17950
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-cysteine + O2
oxidation of cysteine to cysteine sulfinic acid in presence of hercynine or L-histidine
734828
Erwinia tasmaniensis
cysteine sulfinic acid + H2O
-
-
-
?
L-cysteine + O2
oxidation of cysteine to cysteine sulfinic acid in presence of hercynine or L-histidine
734828
Erwinia tasmaniensis DSM 17950
cysteine sulfinic acid + H2O
-
-
-
?
L-cysteine + O2
oxidation of cysteine to cystine
734828
Erwinia tasmaniensis
L-cystine + H2O
-
-
-
?
L-cysteine + O2
oxidation of cysteine to cystine
734828
Erwinia tasmaniensis DSM 17950
L-cystine + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
734828
Erwinia tasmaniensis
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
734828
Erwinia tasmaniensis DSM 17950
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
additional information
the enzyme catalyzes the oxidative coupling between histidine and cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity, NMR spectroscopic product analysis, overview. Enzyme OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine. OvoA-catalyzed reactions can be systematically modulated by a slight modification of one of its substrates, histidine
734828
Erwinia tasmaniensis
?
-
-
-
-
additional information
the enzyme catalyzes the oxidative coupling between histidine and cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity, NMR spectroscopic product analysis, overview. Enzyme OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine. OvoA-catalyzed reactions can be systematically modulated by a slight modification of one of its substrates, histidine
734828
Erwinia tasmaniensis DSM 17950
?
-
-
-
-
Application (protein specific)
Application
Commentary
Organism
synthesis
potential application of the oxidative coupling between hercynine and cysteine for industrial ergothioneine production
Erwinia tasmaniensis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene ovoA, the mutant enzyme loses the cysteine dioxygenase activity but also stops catalyzing the formation of oxidative coupling product
Erwinia tasmaniensis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E176H
site-directed mutagenesis
Erwinia tasmaniensis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
a mononuclear non-heme iron enzyme, dependent on, ligand with 2-His-1-carboxylate facial triad
Erwinia tasmaniensis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-histidine + L-cysteine + O2
Erwinia tasmaniensis
-
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
?
L-histidine + L-cysteine + O2
Erwinia tasmaniensis DSM 17950
-
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hercynine + L-cysteine + O2
-
734828
Erwinia tasmaniensis
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
-
734828
Erwinia tasmaniensis DSM 17950
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-cysteine + O2
oxidation of cysteine to cysteine sulfinic acid in presence of hercynine or L-histidine
734828
Erwinia tasmaniensis
cysteine sulfinic acid + H2O
-
-
-
?
L-cysteine + O2
oxidation of cysteine to cysteine sulfinic acid in presence of hercynine or L-histidine
734828
Erwinia tasmaniensis DSM 17950
cysteine sulfinic acid + H2O
-
-
-
?
L-cysteine + O2
oxidation of cysteine to cystine
734828
Erwinia tasmaniensis
L-cystine + H2O
-
-
-
?
L-cysteine + O2
oxidation of cysteine to cystine
734828
Erwinia tasmaniensis DSM 17950
L-cystine + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
734828
Erwinia tasmaniensis
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
734828
Erwinia tasmaniensis DSM 17950
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
additional information
the enzyme catalyzes the oxidative coupling between histidine and cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity, NMR spectroscopic product analysis, overview. Enzyme OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine. OvoA-catalyzed reactions can be systematically modulated by a slight modification of one of its substrates, histidine
734828
Erwinia tasmaniensis
?
-
-
-
-
additional information
the enzyme catalyzes the oxidative coupling between histidine and cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity, NMR spectroscopic product analysis, overview. Enzyme OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine. OvoA-catalyzed reactions can be systematically modulated by a slight modification of one of its substrates, histidine
734828
Erwinia tasmaniensis DSM 17950
?
-
-
-
-
General Information
General Information
Commentary
Organism
evolution
enzyme OvoA belongs to the 2-His-1-carboxylate catalytic triad type of mononuclear non-heme iron enzymes
Erwinia tasmaniensis
malfunction
mutation of the 2-His-1-carboxylate catalytic triad of the enzyme disrupts the cysteine dioxygenase activity
Erwinia tasmaniensis
metabolism
OvoAis required in ovothiol biosynthesis catalyzing the oxidative coupling between histidine and cysteine
Erwinia tasmaniensis
General Information (protein specific)
General Information
Commentary
Organism
evolution
enzyme OvoA belongs to the 2-His-1-carboxylate catalytic triad type of mononuclear non-heme iron enzymes
Erwinia tasmaniensis
malfunction
mutation of the 2-His-1-carboxylate catalytic triad of the enzyme disrupts the cysteine dioxygenase activity
Erwinia tasmaniensis
metabolism
OvoAis required in ovothiol biosynthesis catalyzing the oxidative coupling between histidine and cysteine
Erwinia tasmaniensis
Other publictions for EC 1.14.99.52
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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Erwinia tasmaniensis, Erwinia tasmaniensis DSM 17950
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Erwinia tasmaniensis
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745960
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Erwinia tasmaniensis
Org. Lett.
16
2122-2125
2014
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734024
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