1.20.4.1: arsenate reductase (glutathione/glutaredoxin)
This is an abbreviated version!
For detailed information about arsenate reductase (glutathione/glutaredoxin), go to the full flat file.
Word Map on EC 1.20.4.1
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1.20.4.1
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arsenite
-
asiii
-
arsr
-
glutaredoxins
-
arsenic-resistant
-
pteris
-
hyperaccumulating
-
metalloid
-
phytochelatins
-
vittata
-
as-contaminated
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cdc25
-
pentavalent
-
arsenate-reducing
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as-resistant
-
frond
-
arsenic-rich
-
arsenate-sensitive
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degradation
-
antimonite
-
arsenic-contaminated
-
monomethylarsonic
- 1.20.4.1
- arsenite
-
asiii
- arsr
- glutaredoxins
-
arsenic-resistant
- pteris
-
hyperaccumulating
-
metalloid
- phytochelatins
- vittata
-
as-contaminated
- cdc25
-
pentavalent
-
arsenate-reducing
-
as-resistant
- frond
-
arsenic-rich
-
arsenate-sensitive
- degradation
- antimonite
-
arsenic-contaminated
-
monomethylarsonic
Reaction
Synonyms
Acr2, Acr2p, ACR3-ArsC, All0195, AR, ARSA, ArsC, arsenate reductase, arsenate reductase (glutaredoxin), AsV reductase, EC 1.97.1.5, gene arsC proteins, glutaredoxin, glutathione:arsenate oxidoreductase, Grx, MXAN_0575, PcAcr2, proteins (specific proteins and subclasses), gene arsC, PvGRX5, reductase, arsenate, slr0946, SynArsC
ECTree
1.20.4.1 arsenate reductase (glutathione/glutaredoxin)Advanced search results
results (
results (Substrates Products
Substrates Products on EC 1.20.4.1 - arsenate reductase (glutathione/glutaredoxin)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
arsenate + glutaredoxin 1
arsenite + glutaredoxin 1 disulfide + H2O
-
-
-
-
r
arsenate + glutaredoxin 2
arsenite + glutaredoxin 1 disulfide + H2O
-
-
-
-
r
arsenate + glutaredoxin 2
arsenite + glutaredoxin 2 disulfide + H2O
-
-
-
-
r
arsenate + glutaredoxin 3
arsenite + glutaredoxin 1 disulfide + H2O
-
-
-
-
r
arsenate + glutaredoxin 3
arsenite + glutaredoxin 3 disulfide + H2O
-
-
-
-
r
arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate
arsenite + glutathione + ?
arsenate + glutaredoxin
arsenite + glutaredoxin disulfide + H2O
-
-
-
-
?
arsenate + glutaredoxin
arsenite + glutaredoxin disulfide + H2O
-
-
-
-
?
arsenate + glutaredoxin
arsenite + glutaredoxin disulfide + H2O
-
-
-
-
?
arsenate + glutaredoxin C7
arsenite + glutaredoxin C7 disulfide + H2O
-
-
-
-
?
arsenate + glutaredoxin C7
arsenite + glutaredoxin C7 disulfide + H2O
-
-
-
-
?
arsenate + glutaredoxin C72.1
arsenite + glutaredoxin C72.1 disulfide + H2O
-
-
-
-
?
arsenate + glutaredoxin C72.1
arsenite + glutaredoxin C72.1 disulfide + H2O
-
-
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
glutaredoxin functions as the electron donor for arsenate reduction
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
glutaredoxin functions as the electron donor for arsenate reduction
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
strong specificity for arsenate
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
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the first step of the reaction is the binding of arsenate, followed by the interaction of the enzyme-arsenate complex with GSH. A reaction scheme is hypothesized in which the enzyme forms a mixed disulfide between the Cys-12 thiolate of ArsC and GSH. Glutaredoxin would then be required to resolve the mixed disulfide, regenerating reduced ArsC
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
thioredoxin is not effective as electron donor
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized 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
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
C12 is located at the active site and is required for catalysis
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
the enzyme is involved in bacterial arsenic resistance
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
the enzyme is involved in bacterial arsenic resistance
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
the enzyme is involved in bacterial arsenic resistance
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
the enzyme is involved in bacterial arsenic resistance
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
the enzyme is involved in bacterial arsenic resistance
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
enzyme catalyzes the oxidation of NADPH coupled with reduction of arsenate in the presence of glutathione reductase, glutathione and glutaredoxin
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
enzyme catalyzes the oxidation of NADPH coupled with reduction of arsenate in the presence of glutathione reductase, glutathione and glutaredoxin
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
thioredoxin is unable to support arsenate reduction. The N-terminal Cys residue is essential for arsenate reductase activity. During the catalytic cycle, Acr2p forms a mixed disulfide with GSH before being reduced vby glutaredoxin to regenerate the active Acr2p reductase
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
-
-
?
arsenate + reduced glutathione
arsenite + glutathione
-
enzyme plays an important role in detoxification of arsenate
-
-
?
arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate
arsenite + glutathione + ?
-
-
-
-
?
arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate
arsenite + glutathione + ?
-
-
-
-
?
additional information
?
-
-
the enzyme exhibits weak phosphatase activity toward 4-nitrophenyl phosphate
-
-
?
additional information
?
-
both glutathione-SH and glutaredoxin are required for activity. No substrate: phosphate
-
-
?
additional information
?
-
-
both glutathione-SH and glutaredoxin are required for activity. No substrate: phosphate
-
-
?
additional information
?
-
-
chemical shift assignments of 1H, 13C and 15N atoms for the reduced form the enzyme
-
-
?
additional information
?
-
chemical shift assignments of 1H, 13C and 15N atoms for the reduced form the enzyme
-
-
?
additional information
?
-
-
the enzyme requires the glutaredoxin system for its reactivation
-
-
?
