BRENDA - Enzyme Database show
show all sequences of 1.20.4.1

Reactivity of glutaredoxins 1,2 and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalazed arsenate reduction

Shi, J.; Vlamis-Gardikas, A.; Aslund, F.; Holmgren, A.; Rosen, B.P.; J. Biol. Chem. 274, 36039-36042 (1999)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
GSH
the enzyme uses GSH with glutaredoxin as electron donor
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.000003
-
glutaredoxin 2
-
Escherichia coli
0.0042
-
glutaredoxin 1
-
Escherichia coli
0.3
-
glutaredoxin 3
-
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arsenate + reduced glutaredoxin
Escherichia coli
the enzyme is involved in bacterial arsenic resistance
arsenite + oxidized glutaredoxin
-
Escherichia coli
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arsenate + reduced glutaredoxin
the enzyme uses GSH with glutaredoxin as electron donor. Glutaredoxin 2 is the most effective hydrogen donor for the reduction of arsenate. During the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase
639367
Escherichia coli
arsenite + oxidized glutaredoxin
-
-
-
-
arsenate + reduced glutaredoxin
the enzyme is involved in bacterial arsenic resistance
639367
Escherichia coli
arsenite + oxidized glutaredoxin
-
639367
Escherichia coli
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.09
-
glutaredoxin 3
-
Escherichia coli
0.14
-
glutaredoxin 2
-
Escherichia coli
0.3
-
glutaredoxin 1
-
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
GSH
the enzyme uses GSH with glutaredoxin as electron donor
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.000003
-
glutaredoxin 2
-
Escherichia coli
0.0042
-
glutaredoxin 1
-
Escherichia coli
0.3
-
glutaredoxin 3
-
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arsenate + reduced glutaredoxin
Escherichia coli
the enzyme is involved in bacterial arsenic resistance
arsenite + oxidized glutaredoxin
-
Escherichia coli
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arsenate + reduced glutaredoxin
the enzyme uses GSH with glutaredoxin as electron donor. Glutaredoxin 2 is the most effective hydrogen donor for the reduction of arsenate. During the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase
639367
Escherichia coli
arsenite + oxidized glutaredoxin
-
-
-
-
arsenate + reduced glutaredoxin
the enzyme is involved in bacterial arsenic resistance
639367
Escherichia coli
arsenite + oxidized glutaredoxin
-
639367
Escherichia coli
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.09
-
glutaredoxin 3
-
Escherichia coli
0.14
-
glutaredoxin 2
-
Escherichia coli
0.3
-
glutaredoxin 1
-
Escherichia coli
Other publictions for EC 1.20.4.1
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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Verma
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6
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Mori
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4
1
1
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1
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727580
Pandey
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Nostoc sp.
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13
43-55
2013
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1
1
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1
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3
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1
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1
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1
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1
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2
1
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1
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1
1
1
1
1
-
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728218
Chaturvedi
Computational identification a ...
Cronobacter sakazakii, Cronobacter sakazakii ATCC BAA-894
J. Struct. Funct. Genomics
14
37-45
2013
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1
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727076
Kim
Redox, mutagenic and structura ...
Synechocystis sp.
Biochim. Biophys. Acta
1824
392-403
2012
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1
1
6
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3
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1
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1
1
6
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1
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714404
Yu
(1)H, (13)C and (15)N resonanc ...
Synechocystis sp.
Biomol. NMR Assign.
5
85-87
2010
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1
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1
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715567
Wu
Novel channel enzyme fusion pr ...
Mycobacterium tuberculosis
J. Biol. Chem.
285
40081-40087
2010
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6
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1
1
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693214
Sundaram
An arsenate-activated glutared ...
Pteris vittata
J. Biol. Chem.
283
6095-6101
2008
1
1
1
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1
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5
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1
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1
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673087
Roos
The activation of electrophile ...
Staphylococcus aureus
Chembiochem
7
981-989
2006
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3
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676606
Ellis
A novel arsenate reductase fro ...
Pteris vittata
Plant Physiol.
141
1544-1554
2006
-
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1
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1
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676858
Dhankher
Hyperaccumulation of arsenic i ...
Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
103
5413-5418
2006
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1
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6
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1
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1
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660258
Duan
Characterization of arsenate r ...
Arabidopsis thaliana, Oryza sativa, Pteris vittata
Plant Physiol.
138
461-469
2005
1
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1
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2
3
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3
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8
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1
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8
7
-
7
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3
1
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3
4
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3
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1
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3
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1
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2
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3
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3
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8
7
-
7
-
3
1
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3
4
-
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677207
Gregus
The glycolytic enzyme glyceral ...
Homo sapiens, Rattus norvegicus
Toxicol. Sci.
85
859-869
2005
-
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8
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3
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639363
Mukhopadhyay
Purification and characterizat ...
Saccharomyces cerevisiae
J. Biol. Chem.
275
21149-21157
2000
1
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1
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2
3
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2
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3
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1
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1
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1
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639367
Shi
Reactivity of glutaredoxins 1, ...
Escherichia coli
J. Biol. Chem.
274
36039-36042
1999
1
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-
3
-
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1
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1
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639364
Liu
Ligand interactions of the Ars ...
Escherichia coli
J. Biol. Chem.
272
21084-21089
1997
1
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3
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639371
Gladysheva
His-8 lowers the pKa of the es ...
Escherichia coli
J. Biol. Chem.
271
33256-33260
1996
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639365
Liu
Identification of an essential ...
Escherichia coli
Biochemistry
34
13472-13476
1995
1
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639366
Gladysheva
Properties of the arsenate red ...
Escherichia coli
Biochemistry
33
7288-7293
1994
1
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3
1
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4
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1
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