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ENZYME entry: EC 1.20.4.1

Accepted Name
Arsenate reductase (glutathione/glutaredoxin).
Alternative Name(s)
Arsenate reductase (glutaredoxin).
Reaction catalysed
Arsenate + glutathione + glutaredoxin <=> arsenite + a glutaredoxin-glutathione disulfide + H(2)O
Cofactor(s)
Mo cation.
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
BRENDA1.20.4.1
EC2PDB1.20.4.1
ExplorEnz1.20.4.1
PRIAM enzyme-specific profiles1.20.4.1
KEGG Ligand Database for Enzyme Nomenclature1.20.4.1
IUBMB Enzyme Nomenclature1.20.4.1
IntEnz1.20.4.1
MEDLINEFind literature relating to 1.20.4.1
MetaCyc1.20.4.1
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;  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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