Arsenate reductase (azurin)
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+
| arsenate reductase (azurin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 | ||||||||
| |||||||||
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.
gollark: Is solarflame being wrong again?
gollark: I decided it was apiohazardous and switched back, although it kept randomly switching me to new reddit for a bit.
gollark: I have, in fact, tried it.
gollark: I *like* the "1998 website" aesthetic.
gollark: It uses unreasonable amounts of client side JS and may actually leak memory while old reddit uses mostly HTML, I have uBO anyway, infinite scrolling means you lose your place if the tab is suspended or whatever and can also trap you in an inescapable reddit cycle, and even "compact" view seems to be wasting space on the sides.
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.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.