ID   1.20.4.1
DE   Arsenate reductase (glutaredoxin).
CA   Arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H(2)O.
CF   Molybdenum.
CC   -!- The glutaredoxins catalyze glutathione-disulfide oxidoreductions and
CC       have a redox-active disulfide/dithiol in the active site (-Cys-
CC       Pro-Tyr-Cys-) that forms a disulfide bond in the oxidized form.
CC   -!- Glutaredoxins have a binding site for glutathione, which is required
CC       to reduce them to the dithiol form.
CC   -!- Thioredoxins reduced by NADPH and thioredoxin reductase can act as
CC       alternative substrates.
CC   -!- The enzyme is part of a system for detoxifying arsenate.
CC   -!- Although the arsenite formed is more toxic than arsenate, it can be
CC       extruded from some bacteria by EC 3.6.3.16.
CC   -!- In other organisms, arsenite can be methylated by EC 2.1.1.137 in a
CC       pathway to non-toxic organoarsenical compounds.
CC   -!- Formerly EC 1.97.1.5.
DR   Q336V5, ACR21_ORYSJ;  Q10SX6, ACR22_ORYSJ;  P08692, ARSC1_ECOLX;
DR   P52147, ARSC2_ECOLX;  P0CF87, ARSCL_ECOLI;  O50595, ARSC_ACIMA ;
DR   P0AB96, ARSC_ECOLI ;  P44589, ARSC_HAEIN ;  P95354, ARSC_NEIGO ;
DR   P63621, ARSC_NEIMA ;  P63622, ARSC_NEIMB ;  P0AB97, ARSC_SHIFL ;
DR   P74984, ARSC_YEREN ;
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