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ENZYME

ENZYME entry: EC 1.20.4.1

Accepted Name
arsenate reductase (glutathione/glutaredoxin)
Alternative Name(s)
arsenate reductase (glutaredoxin)
Reaction catalysed
[glutaredoxin]-dithiol + arsenate + glutathione + H(+) <=> arsenite + glutathionyl-S-S-[glutaredoxin] + H2O
Comment(s)
  • 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; in other organisms, arsenite can be methylated by EC 2.1.1.137 in a pathway that produces non-toxic organoarsenical compounds; cf. EC 1.20.4.4.
  • Formerly EC 1.97.1.5.
Cross-references
BRENDA 1.20.4.1
EC2PDB 1.20.4.1
ExplorEnz 1.20.4.1
PRIAM enzyme-specific profiles 1.20.4.1
KEGG Ligand Database for Enzyme Nomenclature 1.20.4.1
IUBMB Enzyme Nomenclature 1.20.4.1
IntEnz 1.20.4.1
MEDLINE Find literature relating to 1.20.4.1
MetaCyc 1.20.4.1
Rhea expert-curated reactions 1.20.4.1
UniProtKB/Swiss-Prot
Q336V5, ACR21_ORYSJ Q10SX6, ACR22_ORYSJ P08692, ARSC1_ECOLX
P52147, ARSC2_ECOLX P0CF87, ARSCL_ECOLI O50595, ARSC_ACIMA
P0AB96, ARSC_ECOLI P44589, ARSC_HAEIN P95354, ARSC_NEIGO
P63621, ARSC_NEIMA P63622, ARSC_NEIMB Q92R44, ARSC_RHIME
P0AB97, ARSC_SHIFL P74313, ARSC_SYNY3 P74984, ARSC_YEREN
Q6ZEM6, ARSI1_SYNY3 Q6YRW7, ARSI2_SYNY3 Q8GY31, CDC25_ARATH
Q8RUD6, HARC1_ARATH

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