| Accepted Name |
| arsenate reductase (glutathione/glutaredoxin)
|
| Alternative Name(s) |
| arsenate reductase (glutaredoxin) |
| Reaction catalysed |
| [glutaredoxin]-dithiol + arsenate + glutathione + H(+) = glutathionyl-S-S-[glutaredoxin] + arsenite + 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 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.20.4.1 |
| IUBMB Enzyme Nomenclature | 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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