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EC 1.20.4.1 Details
EC number
1.20.4.1
Accepted name
arsenate reductase (glutathione/glutaredoxin)
Reaction
arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O
Other name(s)
ArsC (ambiguous), arsenate:glutaredoxin oxidoreductase, arsenate reductase (glutaredoxin)
Systematic name
arsenate:glutathione/glutaredoxin oxidoreductase
CAS registry number
146907-46-2
Comment
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).
History
created 2000 as EC 1.97.1.5, transferred 2001 to EC 1.20.4.1, modified 2015, modified 2019, modified 2020
EC Tree
1.97.1.5 created 2000 deleted 2001
1.97.1.6 created 2000 deleted 2001
1.97.1.7 created 2000, deleted 2001