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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 |
[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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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.20.4.-
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