| thiocyanate hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 / QuickGO | ||||||||
| |||||||||
A thiocyanate hydrolase (EC 3.5.5.8) is an enzyme belonging to the family of hydrolases. The systematic name of this enzyme class is thiocyanate aminohydrolase. This enzyme catalyzes the chemical reaction:
- SCN− + 2 H2O + H+ ⇌ SCO + NH3
The mechanism is proposed to involve a metal thiocyanate complex.
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.
A second thiocyanate hydrolase with copper at its active site catalyzes its conversion to cyanate:[1]
- SCN− + H2O → OCN− + H2S
References
- ^ Tikhonova, Tamara V.; Sorokin, Dimitry Y.; Hagen, Wilfred R.; Khrenova, Maria G.; Muyzer, Gerard; Rakitina, Tatiana V.; Shabalin, Ivan G.; Trofimov, Anton A.; Tsallagov, Stanislav I.; Popov, Vladimir O. (2020). "Trinuclear Copper Biocatalytic Center Forms an Active Site of Thiocyanate Dehydrogenase". Proceedings of the National Academy of Sciences. 117 (10): 5280–5290. Bibcode:2020PNAS..117.5280T. doi:10.1073/pnas.1922133117. PMID 32094184.
- 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. doi:10.1128/JB.180.10.2583-2589.1998. 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.
