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show all sequences of 1.14.99.52

Regioselectivity of the oxidative C-S bond formation in ergothioneine and ovothiol biosyntheses

Song, H.; Leninger, M.; Lee, N.; Liu, P.; Org. Lett. 15, 4854-4857 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant overexpression of Strep-tagged enzyme in Escherichia coli
Erwinia tasmaniensis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
a mononuclear non-heme iron enzyme, dependent on
Erwinia tasmaniensis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
hercynine + L-cysteine + O2
Erwinia tasmaniensis
-
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
hercynine + L-cysteine + O2
Erwinia tasmaniensis DSM 17950
-
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
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
-
-
?
additional information
Erwinia tasmaniensis
besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
?
-
-
-
additional information
Erwinia tasmaniensis DSM 17950
besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Erwinia tasmaniensis
B2VFD8
gene ovoA
-
Erwinia tasmaniensis DSM 17950
B2VFD8
gene ovoA
-
Purification (Commentary)
Commentary
Organism
recombinant Strep-tagged enzyme from Escherichia coli by affinity chromatography
Erwinia tasmaniensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hercynine + L-cysteine + O2
-
734827
Erwinia tasmaniensis
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
-
734827
Erwinia tasmaniensis DSM 17950
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
734827
Erwinia tasmaniensis
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
734827
Erwinia tasmaniensis DSM 17950
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
additional information
besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
734827
Erwinia tasmaniensis
?
-
-
-
-
additional information
OvoA substrate specificity and substrate binding pocket flexibility, NMR analysis, overview
734827
Erwinia tasmaniensis
?
-
-
-
-
additional information
besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
734827
Erwinia tasmaniensis DSM 17950
?
-
-
-
-
additional information
OvoA substrate specificity and substrate binding pocket flexibility, NMR analysis, overview
734827
Erwinia tasmaniensis DSM 17950
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant overexpression of Strep-tagged enzyme in Escherichia coli
Erwinia tasmaniensis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
a mononuclear non-heme iron enzyme, dependent on
Erwinia tasmaniensis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
hercynine + L-cysteine + O2
Erwinia tasmaniensis
-
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
hercynine + L-cysteine + O2
Erwinia tasmaniensis DSM 17950
-
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
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
-
-
?
additional information
Erwinia tasmaniensis
besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
?
-
-
-
additional information
Erwinia tasmaniensis DSM 17950
besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant Strep-tagged enzyme from Escherichia coli by affinity chromatography
Erwinia tasmaniensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hercynine + L-cysteine + O2
-
734827
Erwinia tasmaniensis
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
-
734827
Erwinia tasmaniensis DSM 17950
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
734827
Erwinia tasmaniensis
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
734827
Erwinia tasmaniensis DSM 17950
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
additional information
besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
734827
Erwinia tasmaniensis
?
-
-
-
-
additional information
OvoA substrate specificity and substrate binding pocket flexibility, NMR analysis, overview
734827
Erwinia tasmaniensis
?
-
-
-
-
additional information
besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
734827
Erwinia tasmaniensis DSM 17950
?
-
-
-
-
additional information
OvoA substrate specificity and substrate binding pocket flexibility, NMR analysis, overview
734827
Erwinia tasmaniensis DSM 17950
?
-
-
-
-
General Information
General Information
Commentary
Organism
evolution
the two known sulfoxide synthases EgtB and OvoA distinguish themselves from each other by their substrate preferences and product C-S bond regioselectivity
Erwinia tasmaniensis
metabolism
the enzyme is involved in the ergothioneine and ovothiol biosynthesis. Besides catalyzing the oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps, overview
Erwinia tasmaniensis
physiological function
ovothiol is proposed to be involved in H2O2 scavenging and facilitating the fertilization process
Erwinia tasmaniensis
General Information (protein specific)
General Information
Commentary
Organism
evolution
the two known sulfoxide synthases EgtB and OvoA distinguish themselves from each other by their substrate preferences and product C-S bond regioselectivity
Erwinia tasmaniensis
metabolism
the enzyme is involved in the ergothioneine and ovothiol biosynthesis. Besides catalyzing the oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps, overview
Erwinia tasmaniensis
physiological function
ovothiol is proposed to be involved in H2O2 scavenging and facilitating the fertilization process
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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1
2
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Erwinia tasmaniensis, Erwinia tasmaniensis DSM 17950
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1
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6
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10
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1
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1
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1
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2
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10
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3
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743388
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Erwinia tasmaniensis
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1
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745960
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Erwinia tasmaniensis
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1
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2
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49
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2
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1
1
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1
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5
1
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2
2
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6
734827
Song
Regioselectivity of the oxidat ...
Erwinia tasmaniensis, Erwinia tasmaniensis DSM 17950
Org. Lett.
15
4854-4857
2013
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3
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733972
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Erwinia tasmaniensis, Erwinia tasmaniensis DSM 17950
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51
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734024
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133
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