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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

Reaction

arsenate
+
glutathione
+
glutaredoxin
=
arsenite
+
a glutaredoxin-glutathione disulfide
+
H2O

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 Oxidoreductases
         1.20 Acting on phosphorus or arsenic in donors
             1.20.4 With disulfide as acceptor
                1.20.4.1 arsenate reductase (glutathione/glutaredoxin)

Crystallization

Crystallization on EC 1.20.4.1 - arsenate reductase (glutathione/glutaredoxin)

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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