Mercury(II) reductase
| mercury (II) reductase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 1.16.1.1 | ||||||
| CAS number | 67880-93-7 | ||||||
| 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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In enzymology, a mercury(II) reductase (EC 1.16.1.1) is an enzyme that catalyzes the chemical reaction
- Hg + NADP+ + H+
Hg2+ + NADPH
The 3 substrates of this enzyme are Hg, NADP+, and H+, whereas its two products are Hg2+ and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those oxidizing metal ion with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is Hg:NADP+ oxidoreductase. Other names in common use include mercuric reductase, mercurate(II) reductase, mercuric ion reductase, mercury reductase, reduced NADP+:mercuric ion oxidoreductase, and mer A.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1ZK7 and 1ZX9. A low resolution (>3.9 Å) was solved in 1991.[1]
References
- ^ Schiering N, Kabsch W, Moore MJ, Distefano MD, Walsh CT, Pai EF (July 1991). "Structure of the detoxification catalyst mercuric ion reductase from Bacillus sp. strain RC607". Nature 352 (6331): 168–72. doi:10.1038/352168a0. PMID 2067577.
Further reading
- Fox B, Walsh CT (1982). "Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide". J. Biol. Chem. 257 (5): 2498–503. PMID 6277900.
- Fox, BS and Walsh CT (1983). "Mercuric reductase - homology to glutathione-reductase and lipoamide dehydrogenase - iodoacetamide alkylation and sequence of the active-site peptide". Biochemistry 22 (17): 4082–4088. doi:10.1021/bi00286a014. PMID 6412751.