ENZYME entry: EC 184.108.40.206
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|Arsenate reductase (glutathione/glutaredoxin).
|Arsenate reductase (glutaredoxin).|
|Arsenate + glutathione + glutaredoxin <=> arsenite + a glutaredoxin-glutathione disulfide + H(2)O|
- 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 220.127.116.11; in other organisms,
arsenite can be methylated by EC 18.104.22.168 in a pathway that produces
non-toxic organoarsenical compounds; cf. EC 22.214.171.124.
- Formerly EC 126.96.36.199.
|PRIAM enzyme-specific profiles||188.8.131.52|
|KEGG Ligand Database for Enzyme Nomenclature||184.108.40.206|
|IUBMB Enzyme Nomenclature||220.127.116.11|
|MEDLINE||Find literature relating to 18.104.22.168|
|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; |
entries corresponding to 1.20.4.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.20.-.-
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