| arsenate reductase (azurin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.20.9.1 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
Arsenate reductase (azurin) (EC 1.20.9.1) 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 oxidised azurin, whereas its 3 products are arsenate, reduced azurin, and hydrogen ion.
Classification
This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with a copper protein as acceptor.
Nomenclature
The systematic name of this enzyme class is arsenite:azurin oxidoreductase. This enzyme is also called arsenite oxidase.
Structure and function
The enzyme contains a molybdopterin centre comprising two molybdopterin guanosine dinucleotide cofactors bound to molybdenum, a [3Fe-4S] cluster and a Rieske-type [2Fe-2S] cluster. Also uses a c-type cytochrome or O
2 as acceptors.
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 (2001). "Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A". Structure. 9 (2): 125–32. doi:10.1016/S0969-2126(01)00566-4. PMID 11250197.
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