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Information on EC 1.20.4.1 - arsenate reductase (glutathione/glutaredoxin) and Organism(s) Synechocystis sp. and UniProt Accession P74313

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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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This record set is specific for:
Synechocystis sp.
UNIPROT: P74313
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The taxonomic range for the selected organisms is: Synechocystis sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide
arsenate
+
glutathione
+
glutaredoxin
=
arsenite
+
a glutaredoxin-glutathione disulfide
+
H2O
+
+
=
+
a glutaredoxin-glutathione disulfide
+
Synonyms
arsenate reductase, asv reductase, acr2p, pvgrx5, slr0946, synarsc, all0195, pcacr2, mxan_0575, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acr2p
-
-
-
-
ArsC
-
-
-
-
arsenate reductase
-
-
arsenate reductase (glutaredoxin)
-
-
-
-
gene arsC proteins
-
-
-
-
glutathione:arsenate oxidoreductase
-
-
-
-
proteins (specific proteins and subclasses), gene arsC
-
-
-
-
reductase, arsenate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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).
CAS REGISTRY NUMBER
COMMENTARY hide
146907-46-2
-
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 glutaredoxin
arsenite + oxidized glutaredoxin
show the reaction diagram
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-
-
?
additional information
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutaredoxin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002
arsenate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14400
x * 14400, SDS-PAGE
15000
x * 15000, SDS-PAGE, x* 15507, MALDI-TOF, His-tagged recombinant protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in silico modeling of disulfide bonds into the solution NMR structure of the fully-reduced enzyme. C8/C82 and C80C82 disulfides are equally consistent
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C13A
114% of wild-type vmax
C35A
l00% of wild-type vmax
C80A
less than 2% of wild-type vmax
C80A/C82A
less than 2% of wild-type vmax
C82A
less than 2% of wild-type vmax
C8A
less than 2% of wild-type vmax
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography, gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yu, C.; Xia, B.; Jin, C.
(1)H, (13)C and (15)N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803
Biomol. NMR Assign.
5
85-87
2010
Synechocystis sp., Synechocystis sp. (P74313)
Manually annotated by BRENDA team
Kim, S.G.; Chung, J.S.; Sutton, R.B.; Lee, J.S.; Lopez-Maury, L.; Lee, S.Y.; Florencio, F.J.; Lin, T.; Zabet-Moghaddam, M.; Wood, M.J.; Nayak, K.; Madem, V.; Tripathy, J.N.; Kim, S.K.; Knaff, D.B.
Redox, mutagenic and structural studies of the glutaredoxin/arsenate reductase couple from the cyanobacterium Synechocystis sp. PCC 6803
Biochim. Biophys. Acta
1824
392-403
2012
Synechocystis sp. (P74313), Synechocystis sp.
Manually annotated by BRENDA team