Arsenate reductase (azurin)
From Wikipedia, the free encyclopedia
| arsenate reductase (azurin) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 1.20.98.1 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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Arsenate reductase (azurin) (EC 1.20.98.1) is an enzyme that catalyzes the chemical reaction
- arsenite + H2O + 2 azurinox
arsenate + 2 azurinred + 2 H+
The 3 substrates of this enzyme are arsenite, water, and azurinox, whereas its 3 products are arsenate, azurinred, and hydrogen ion.
This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with other, known, acceptors. The systematic name of this enzyme class is arsenite:azurin oxidoreductase. This enzyme is also called arsenite oxidase.
[edit] References
- Anderson GL, Williams J, Hille R (1992). "The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase". J. Biol. Chem. 267 (33): 23674–82. PMID 1331097.
- Ellis PJ, Conrads T, Hille R, Kuhn P (Camb). "Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A". S Structure. (2): 125–32. PMID 11250197.
arsenate + 2 azurinred + 2 H+