Information on EC 1.20.4.1 - arsenate reductase (glutaredoxin)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.20.4.1
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RECOMMENDED NAME
GeneOntology No.
arsenate reductase (glutaredoxin)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
arsenate detoxification I (glutaredoxin)
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arsenate detoxification II (glutaredoxin)
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non-pathway related
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SYSTEMATIC NAME
IUBMB Comments
arsenate:glutaredoxin oxidoreductase
A molybdoenzyme. The enzyme is part of a system for detoxifying arsenate. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 3.6.3.16, 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).
CAS REGISTRY NUMBER
COMMENTARY hide
146907-46-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
glyceraldehyde-3-phosphate dehydrogenase working as arsenate reductase
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
Nostoc sp. PCC7120
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UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
glyceraldehyde-3-phosphate dehydrogenase working as arsenate reductase
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arsenate + reduced acceptor
arsenite + acceptor
show the reaction diagram
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
show the reaction diagram
arsenate + reduced glutathione
arsenite + glutathione
show the reaction diagram
arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate
arsenite + glutathione + ?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
arsenate + reduced acceptor
arsenite + acceptor
show the reaction diagram
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
show the reaction diagram
arsenate + reduced glutathione
arsenite + glutathione
show the reaction diagram
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enzyme plays an important role in detoxification of arsenate
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutaredoxin
glutathione
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenite
diethyldicarbonate
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-
iodoacetate
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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
phosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenate
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10 mM increases enzyme activity by 1.6fold
additional information
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enzyme is arsenate-inducible
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002 - 28
arsenate
0.000002 - 0.0006
glutaredoxin
0.0042
glutaredoxin 1
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-
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0.000003
glutaredoxin 2
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-
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0.3
glutaredoxin 3
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0.57
reduced glutathione
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pH 6.5, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
glutaredoxin 1
Escherichia coli
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-
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0.14
glutaredoxin 2
Escherichia coli
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0.09
glutaredoxin 3
Escherichia coli
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.45
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root
3.84
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shoot
4.8
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isolated roots in arsenate containiing culture medium, basic level
24
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isolated roots in arsenate containiing culture medium, induced for 9 h by arsenate
additional information
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in vivo activity after feeding experiments
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 6.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7
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5.5 - 7.5
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90% of maximal activity at pH 5.5, 60% at pH 7.5
5.5
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90% of maximum activity
7.5
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60% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
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broad optimum
additional information
-
reductase activity increases from 10C to 40C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
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; broad
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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enzyme activity is constitutive and unaffected by presence of arsenate
Manually annotated by BRENDA team
additional information
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no activity in shoot, arsenite is the main storage form in the fern fronds; no enzymic activity in shoots
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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besides glyceraldehyde-3-phosphate dehydrogenase, presence of other enzymes contributing to arsenate reduction
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 16822, calculation from nucleotide sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molecular modeing of structure. Residues Cys12, Arg60, Arg94, and Arg107 are identified as metal binding residues
comparative homology modeling. Along with Cys11, the residues like Ile8, Pro9, Asn10, Gly12, Thr13, Cys14, Lys15, and Phe18 also show coordination with arsenate; molecular modeling and docking with asenate oxyanion. Residues Cys11, Ile8, Pro9, Asn10, Gly12, Thr13, Cys14, Lys15, and Phe18 show coordination with arsenate
in silico modeling of disulfide bonds into the solution NMR structure of the fully-reduced enzyme. C8/C82 and C80C82 disulfides are equally consistent
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
stable up to
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity purified
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using Ni-NTA chromatography, gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli
cloned into the bacterial expression vector and expressed in Escherichia coli as a C-terminal histidine-tagged protein
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expressed in Escherichia coli as a His-tagged fusion protein
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expression in Escherichia coli
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expression in Escherichia coli complements phenotypes
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gene Pv5-6 encoding PvGrx5 expressed in Escherichia coli strain XL-1 Blue. PvGrx5 expressed in Escherichia coli mutants in which the arsenic resistance genes of the ars operon are deleted (strain AW3110), a deletion of the gene for the ArsC arsenate reductase (strain WC3110), and a strain in which the ars operon is deleted and the gene for the GlpF aquaglyceroporin is disrupted (strain OSBR1)
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sequence contains a variation of conserved motif HCX5R where R is replaced by S
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enhanced expression under sodium arsenate stress
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A11W
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same Km for arsenate as the wild type with maximal velocity approximately half that of the wild type enzyme
A11W/C12S
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catalytic inactive mutation
C106G
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the maximal velocity is approximately half that of the wild type enzyme
C12S
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catalytically inactive mutant
Y7W
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same Km and maximal velocity as the wild type
C67A
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loss of both GRX activity and arsenic resistance
N13A
decrease in activity due to lower local softness, analysis of S-As bond length, Wiberg bond orders, lewaving group energy and nucleofugality
R16A
decrease in activity due to lower local softness, analysis of S-As bond length, Wiberg bond orders, lewaving group energy and nucleofugality
S17A
decrease in activity due to lower local softness, analysis of S-As bond length, Wiberg bond orders, lewaving group energy and nucleofugality
C13A
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114% of wild-type vmax
C35A
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l00% of wild-type vmax
C80A
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less than 2% of wild-type vmax
C80A/C82A
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less than 2% of wild-type vmax
C82A
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less than 2% of wild-type vmax
C8A
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less than 2% of wild-type vmax
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
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PvGrx5 has a role in regulating intracellular arsenite levels, by either directly or indirectly modulating the aquaglyceroporin
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