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Information on EC 1.20.4.1 - arsenate reductase (glutathione/glutaredoxin)
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1.20.4.1 arsenate reductase (glutathione/glutaredoxin)IUBMB Comments
The enzyme is part of a system for detoxifying arsenate. The substrate binds to a catalytic cysteine residue, forming a covalent thiolate---As(V) intermediate. A tertiary intermediate is then formed between the arsenic, the enzyme's cysteine, and a glutathione cysteine. This intermediate is reduced by glutaredoxin, which forms a dithiol with the glutathione, leading to the dissociation of arsenite. Thus reduction of As(V) is mediated by three cysteine residues: one in ArsC, one in glutathione, and one in glutaredoxin. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 7.3.2.7, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. cf. EC 1.20.4.4, arsenate reductase (thioredoxin).
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Word Map
- 1.20.4.1
- arsenite
-
asiii
- arsr
- glutaredoxins
-
arsenic-resistant
- pteris
-
hyperaccumulating
-
metalloid
- phytochelatins
- vittata
-
as-contaminated
- cdc25
-
pentavalent
-
arsenate-reducing
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as-resistant
- frond
-
arsenic-rich
-
arsenate-sensitive
- degradation
- antimonite
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arsenic-contaminated
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monomethylarsonic
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
=
+
a glutaredoxin-glutathione disulfide
+
Synonyms
arsenate reductase, asv reductase, acr2p, pvgrx5, slr0946, synarsc, all0195, pcacr2, mxan_0575, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acr2
Acr2p
-
-
-
-
ACR3-ArsC
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gene name, protein comprises two domains an aquaglyceroporin-derived N-terminal channel-like part fused to a C-terminal enzyme domain with similarity to ArsC arsenate reductase
All0195
AR
ArsC
arsenate reductase
arsenate reductase (glutaredoxin)
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-
-
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AsV reductase
EC 1.97.1.5
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formerly
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gene arsC proteins
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-
-
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glutathione:arsenate oxidoreductase
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-
-
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proteins (specific proteins and subclasses), gene arsC
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-
-
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reductase, arsenate
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-
-
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ArsC
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O
arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O
-
-
-
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arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O
reaction mechanism
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arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O
arsenate reduction by glyceraldehyde-3-phosphate dehydrogenase may take place during or as a consequence of, the arsenolytic cleavage of the thioester bond formed between the enzymes C149 and the 3-phosphoglycerol moiety of the substrate
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arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O
first reaction step is a nucleophilic displacement reaction by C10 on dianionic arsenate. Second step is a preferential nucleophilic attack of C82 on the monoanionic C10-arsenate intermediate stabilized by S17. Thiolate form of C82 is stabilized by an eight-residue alpha helix flanked by C82 and C89 and a hydrogen bond with T11. during the final step, C89 is activated as a nucleophile by structural alterations of the redox helix
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
arsenate:glutathione/glutaredoxin oxidoreductase
The enzyme is part of a system for detoxifying arsenate. The substrate binds to a catalytic cysteine residue, forming a covalent thiolate---As(V) intermediate. A tertiary intermediate is then formed between the arsenic, the enzyme's cysteine, and a glutathione cysteine. This intermediate is reduced by glutaredoxin, which forms a dithiol with the glutathione, leading to the dissociation of arsenite. Thus reduction of As(V) is mediated by three cysteine residues: one in ArsC, one in glutathione, and one in glutaredoxin. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 7.3.2.7, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. cf. EC 1.20.4.4, arsenate reductase (thioredoxin).
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CAS REGISTRY NUMBER
COMMENTARY
146907-46-2
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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
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-
-
-
?
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
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-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
glutaredoxin functions as the electron donor for arsenate reduction
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-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
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strong specificity for arsenate
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-
?
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
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-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
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thioredoxin is not effective as electron donor
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-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
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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
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-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
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C12 is located at the active site and is required for catalysis
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?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
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the enzyme is involved in bacterial arsenic resistance
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?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
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the enzyme is involved in bacterial arsenic resistance
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?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
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the enzyme is involved in bacterial arsenic resistance
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
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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
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-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
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-
-
?
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
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-
-
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
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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
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-
-
?
arsenate + reduced glutathione
arsenite + glutathione
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enzyme plays an important role in detoxification of arsenate
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-
?
arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate
arsenite + glutathione + ?
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-
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?
arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate
arsenite + glutathione + ?
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-
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?
additional information
?
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the enzyme exhibits weak phosphatase activity toward 4-nitrophenyl phosphate
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-
?
additional information
?
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both glutathione-SH and glutaredoxin are required for activity. No substrate: phosphate
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?
additional information
?
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both glutathione-SH and glutaredoxin are required for activity. No substrate: phosphate
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?
additional information
?
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chemical shift assignments of 1H, 13C and 15N atoms for the reduced form the enzyme
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-
?
additional information
?
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chemical shift assignments of 1H, 13C and 15N atoms for the reduced form the enzyme
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?
additional information
?
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the enzyme requires the glutaredoxin system for its reactivation
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-
?
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NATURAL SUBSTRATE
NATURAL 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 + reduced glutathione
arsenite + glutathione
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enzyme plays an important role in detoxification of arsenate
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-
?
arsenate + glutaredoxin
arsenite + glutaredoxin disulfide + H2O
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-
-
-
?
arsenate + glutaredoxin
arsenite + glutaredoxin disulfide + H2O
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-
-
-
?
arsenate + glutaredoxin
arsenite + glutaredoxin disulfide + H2O
-
-
-
-
?
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
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutaredoxin
replacement of the active-site Cys15 by serine completely eliminates the ability of glutatredoxin A to serve as an electron donor. Replacement of either of the two cysteine residues distant from the active site, i.e., Cys 36 and Cys70, has no effect on the electron-donating ability of glutaredoxin
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme is not stimulated by 1 mM MgCl2, MnCl2, CuCl2, CaCl2, ZnCl2, NiCl2, FeCl2 or FeCl3
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetate
-
inactivates wild type enzyme and mutant enzyme C106S, in presence of substrate, arsenate, or the competitive inhibitors phosphate or sulfate, the rate of the alkylation is reduced
Koningic acid
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inhibition of both classical enzymic and arsentate reductase activities of glyceraldehyde-3-phosphate dehydrogenase
Koningic acid
-
inhibition of both classical enzymic and arsentate reductase activities of glyceraldehyde-3-phosphate dehydrogenase
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
enzyme activity is increased about 1.5fold by the addition of 2 mM dithiothreitol
additional information
-
1 mM EDTA has no apparent effect on enzyme activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Communicable Diseases
Pathogens and gene product normalization in the biomedical literature.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0002
arsenate
wild-type, pH 7.5, temperature not specified in the publication
0.0002
arsenate
mutant C13A, pH 7.5, temperature not specified in the publication
0.0002
arsenate
mutant C35A, pH 7.5, temperature not specified in the publication
0.0006
glutaredoxin
-
glutaredoxin 1p from Saccharomyces cerevisiae or glutaredoxin 1 from E. coli
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24
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isolated roots in arsenate containiing culture medium, induced for 9 h by arsenate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
glyceraldehyde-3-phosphate dehydrogenase working as arsenate reductase
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-
brenda
glyceraldehyde-3-phosphate dehydrogenase working as arsenate reductase
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brenda
5fold increase in enzyme activity after 9 days treatment with 2 mM arsenate
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brenda
ArsC protein from cyanobacterium Synechocystis sp. strain PCC 6803 (SynArsC) is related to the thioredoxin-dependent ArsC family, but uses the glutathione/glutaredoxin system for arsenate reduction (thioredoxin/glutaredoxin hybrid arsenate reductase)
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
enzyme activity is constitutive and unaffected by presence of arsenate
brenda
additional information
additional information
-
no activity in shoot, arsenite is the main storage form in the fern fronds
brenda
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