Thiocyanate hydrolase
| thiocyanate hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.5.8 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a thiocyanate hydrolase (EC 3.5.5.8) is an enzyme that catalyzes the chemical reaction
- thiocyanate + 2 H2O carbonyl sulfide + NH3 + HO-
Thus, the two substrates of this enzyme are thiocyanate and H2O, whereas its 3 products are carbonyl sulfide, NH3, and HO-.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. The systematic name of this enzyme class is thiocyanate aminohydrolase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 2DD4, 2DD5, 2DXB, and 2DXC.
References
- Katayama Y, Matsushita Y, Kaneko M, Kondo M, Mizuno T, Nyunoya H (1998). "Cloning of genes coding for the three subunits of thiocyanate hydrolase of Thiobacillus thioparus THI 115 and their evolutionary relationships to nitrile hydratase". J. Bacteriol. 180 (10): 2583–9. PMC 107207
. PMID 9573140. - Katayama Y, Narahara Y, Inoue Y, Amano F, Kanagawa T, Kuraishi H (1992). "A thiocyanate hydrolase of Thiobacillus thioparus. A novel enzyme catalyzing the formation of carbonyl sulfide from thiocyanate". J. Biol. Chem. 267 (13): 9170–5. PMID 1577754.
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