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arsenate + glutaredoxin
arsenite + glutaredoxin disulfide + H2O
arsenate + glutaredoxin 1
arsenite + glutaredoxin 1 disulfide + H2O
-
Substrates: -
Products: -
r
arsenate + glutaredoxin 2
arsenite + glutaredoxin 1 disulfide + H2O
-
Substrates: -
Products: -
r
arsenate + glutaredoxin 2
arsenite + glutaredoxin 2 disulfide + H2O
-
Substrates: -
Products: -
r
arsenate + glutaredoxin 3
arsenite + glutaredoxin 1 disulfide + H2O
-
Substrates: -
Products: -
r
arsenate + glutaredoxin 3
arsenite + glutaredoxin 3 disulfide + H2O
-
Substrates: -
Products: -
r
arsenate + glutaredoxin C7
arsenite + glutaredoxin C7 disulfide + H2O
arsenate + glutaredoxin C72.1
arsenite + glutaredoxin C72.1 disulfide + H2O
arsenate + glutathione
arsenite + glutathione disulfide + H2O
-
Substrates: -
Products: -
?
arsenate + reduced acceptor
arsenite + acceptor
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
arsenate + reduced glutathione
arsenite + glutathione
arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate
arsenite + glutathione + ?
arsenite + acceptor
arsenate + reduced acceptor
-
Substrates: high activity
Products: -
?
additional information
?
-
arsenate + glutaredoxin
arsenite + glutaredoxin disulfide + H2O
-
Substrates: -
Products: -
?
arsenate + glutaredoxin
arsenite + glutaredoxin disulfide + H2O
-
Substrates: -
Products: -
?
arsenate + glutaredoxin
arsenite + glutaredoxin disulfide + H2O
-
Substrates: -
Products: -
?
arsenate + glutaredoxin
arsenite + glutaredoxin disulfide + H2O
-
Substrates: -
Products: -
?
arsenate + glutaredoxin C7
arsenite + glutaredoxin C7 disulfide + H2O
-
Substrates: -
Products: -
?
arsenate + glutaredoxin C7
arsenite + glutaredoxin C7 disulfide + H2O
-
Substrates: -
Products: -
?
arsenate + glutaredoxin C72.1
arsenite + glutaredoxin C72.1 disulfide + H2O
-
Substrates: -
Products: -
?
arsenate + glutaredoxin C72.1
arsenite + glutaredoxin C72.1 disulfide + H2O
-
Substrates: -
Products: -
?
arsenate + reduced acceptor
arsenite + acceptor
-
Substrates: -
Products: -
?
arsenate + reduced acceptor
arsenite + acceptor
-
Substrates: -
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
Substrates: glutaredoxin functions as the electron donor for arsenate reduction
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
Substrates: glutaredoxin functions as the electron donor for arsenate reduction
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
Substrates: strong specificity for arsenate
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
Substrates: 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
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
Substrates: thioredoxin is not effective as electron donor
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
Substrates: 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
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
Substrates: C12 is located at the active site and is required for catalysis
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
Substrates: the enzyme is involved in bacterial arsenic resistance
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
Substrates: -
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
Substrates: enzyme catalyzes the oxidation of NADPH coupled with reduction of arsenate in the presence of glutathione reductase, glutathione and glutaredoxin
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
Substrates: -
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
Substrates: enzyme catalyzes the oxidation of NADPH coupled with reduction of arsenate in the presence of glutathione reductase, glutathione and glutaredoxin
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
Substrates: -
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
-
Substrates: 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
Products: -
?
arsenate + reduced glutaredoxin
arsenite + oxidized glutaredoxin
Substrates: -
Products: -
?
arsenate + reduced glutathione
arsenite + glutathione
-
Substrates: -
Products: -
?
arsenate + reduced glutathione
arsenite + glutathione
-
Substrates: -
Products: -
?
arsenate + reduced glutathione
arsenite + glutathione
-
Substrates: -
Products: -
?
arsenate + reduced glutathione
arsenite + glutathione
Substrates: -
Products: -
?
arsenate + reduced glutathione
arsenite + glutathione
-
Substrates: enzyme plays an important role in detoxification of arsenate
Products: -
?
arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate
arsenite + glutathione + ?
-
Substrates: -
Products: -
?
arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate
arsenite + glutathione + ?
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme exhibits weak phosphatase activity toward 4-nitrophenyl phosphate
Products: -
?
additional information
?
-
Substrates: both glutathione-SH and glutaredoxin are required for activity. No substrate: phosphate
Products: -
?
additional information
?
-
-
Substrates: both glutathione-SH and glutaredoxin are required for activity. No substrate: phosphate
Products: -
?
additional information
?
-
-
Substrates: no substrate: phosphate, nitrate
Products: -
?
additional information
?
-
-
Substrates: chemical shift assignments of 1H, 13C and 15N atoms for the reduced form the enzyme
Products: -
?
additional information
?
-
Substrates: chemical shift assignments of 1H, 13C and 15N atoms for the reduced form the enzyme
Products: -
?
additional information
?
-
-
Substrates: the enzyme requires the glutaredoxin system for its reactivation
Products: -
?
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Mukhopadhyay, R.; Shi, J.; Rosen, B.P.
Purification and characterization of Acr2p, the Saccharomyces cerevisiae arsenate reductase
J. Biol. Chem.
275
21149-21157
2000
Saccharomyces cerevisiae
brenda
Liu, J.; Rosen, B.P.
Ligand interactions of the ArsC arsenate reductase
J. Biol. Chem.
272
21084-21089
1997
Escherichia coli
brenda
Liu, J.; Gladysheva, T.B.; Lee, L.; Rosen, B.P.
Identification of an essential cysteinyl residue in the ArsC arsenate reductase of plasmid R773
Biochemistry
34
13472-13476
1995
Escherichia coli
brenda
Gladysheva, T.B.; Oden, K.L.; Rosen, B.P.
Properties of the arsenate reductase of plasmid R773
Biochemistry
33
7288-7293
1994
Escherichia coli
brenda
Shi, J.; Vlamis-Gardikas, A.; Aslund, F.; Holmgren, A.; Rosen, B.P.
Reactivity of glutaredoxins 1,2 and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalazed arsenate reduction
J. Biol. Chem.
274
36039-36042
1999
Escherichia coli
brenda
Gladysheva, T.; Liu, J.; Rosen, B.P.
His-8 lowers the pKa of the essential Cys-12 residue of the ArsC arsenate reductase of plasmid R773
J. Biol. Chem.
271
33256-33260
1996
Escherichia coli
brenda
Duan, G.L.; Zhu, Y.G.; Tong, Y.P.; Cai, C.; Kneer, R.
Characterization of arsenate reductase in the extract of roots and fronds of Chinese brake fern, an arsenic hyperaccumulator
Plant Physiol.
138
461-469
2005
Arabidopsis thaliana, Oryza sativa, Pteris vittata
brenda
Roos, G.; Loverix, S.; Brosens, E.; Van Belle, K.; Wyns, L.; Geerlings, P.; Messens, J.
The activation of electrophile, nucleophile and leaving group during the reaction catalysed by pI258 arsenate reductase
Chembiochem
7
981-989
2006
Staphylococcus aureus (P0A006)
brenda
Ellis, D.R.; Gumaelius, L.; Indriolo, E.; Pickering, I.J.; Banks, J.A.; Salt, D.E.
A novel arsenate reductase from the arsenic hyperaccumulating fern Pteris vittata
Plant Physiol.
141
1544-1554
2006
Pteris vittata (Q1A5X4), Pteris vittata
brenda
Dhankher, O.P.; Rosen, B.P.; McKinney, E.C.; Meagher, R.B.
Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced for arsenate reductase (ACR2)
Proc. Natl. Acad. Sci. USA
103
5413-5418
2006
Arabidopsis thaliana
brenda
Gregus, Z.; Nemeti, B.
The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase works as an arsenate reductase in human red blood cells and rat liver cytosol
Toxicol. Sci.
85
859-869
2005
Homo sapiens, Rattus norvegicus
brenda
Sundaram, S.; Rathinasabapathi, B.; Ma, L.Q.; Rosen, B.P.
An arsenate-activated glutaredoxin from the arsenic hyperaccumulator fern Pteris vittata L. regulates intracellular arsenite
J. Biol. Chem.
283
6095-6101
2008
Pteris vittata (Q1A5X4), Pteris vittata
brenda
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)
brenda
Wu, B.; Song, J.; Beitz, E.
Novel channel enzyme fusion proteins confer arsenate resistance
J. Biol. Chem.
285
40081-40087
2010
Mycobacterium tuberculosis
brenda
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.
brenda
Pandey, S.; Shrivastava, A.K.; Singh, V.K.; Rai, R.; Singh, P.K.; Rai, S.; Rai, L.C.
A new arsenate reductase involved in arsenic detoxification in Anabaena sp. PCC7120
Funct. Integr. Genomics
13
43-55
2013
Nostoc sp. (Q8Z0A3), Nostoc sp. PCC 7120 (Q8Z0A3)
brenda
Chaturvedi, N.; Singh, V.K.; Pandey, P.N.
Computational identification and analysis of arsenate reductase protein in Cronobacter sakazakii ATCC BAA-894 suggests potential microorganism for reducing arsenate
J. Struct. Funct. Genomics
14
37-45
2013
Cronobacter sakazakii (A7MRG2), Cronobacter sakazakii, Cronobacter sakazakii ATCC BAA-894 (A7MRG2), Cronobacter sakazakii ATCC BAA-894
brenda
Hu, C.; Yu, C.; Liu, Y.; Hou, X.; Liu, X.; Hu, Y.; Jin, C.
A hybrid mechanism for the Synechocystis arsenate reductase revealed by structural snapshots during arsenate reduction
J. Biol. Chem.
290
22262-22273
2015
Synechocystis sp. PCC 6803
brenda
Mori, Y.; Kimura, Y.
Myxococcus xanthus low-molecular-weight protein tyrosine phosphatase homolog, ArsA, possesses arsenate reductase activity
J. Biosci. Bioeng.
118
10-13
2014
Myxococcus xanthus
brenda
Verma, P.K.; Verma, S.; Meher, A.K.; Pande, V.; Mallick, S.; Bansiwal, A.K.; Tripathi, R.D.; Dhankher, O.P.; Chakrabarty, D.
Overexpression of rice glutaredoxins (OsGrxs) significantly reduces arsenite accumulation by maintaining glutathione pool and modulating aquaporins in yeast
Plant Physiol. Biochem.
106
208-217
2016
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda