EC number:3.5.5.8

Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.5 In nitriles
ID:3.5.5.8
Description:Thiocyanate hydrolase.
Cath: 1.10.472.20; 3.90.330.10; 2.30.30.50;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.5.8
BRENDA Enzyme Link: BRENDA 3.5.5.8
KEGG Enzyme Link: KEGG3.5.5.8
BioCyc Enzyme Link: BioCyc 3.5.5.8
ExPASy Enzyme Link: ExPASy3.5.5.8
EC2PDB Enzyme Link: EC2PDB 3.5.5.8
ExplorEnz Enzyme Link: ExplorEnz 3.5.5.8
PRIAM enzyme-specific profiles Link: PRIAM 3.5.5.8
IntEnz Enzyme Link: IntEnz 3.5.5.8
MEDLINE Enzyme Link: MEDLINE 3.5.5.8

EC number:3.5.5.8

MSA:

3.5.5.8;
Phylogenetic Tree:

3.5.5.8;
Uniprot:
M-CSA:
RHEA:21464 2 H(+) + H2O + thiocyanate = carbonyl sulfide + NH4(+)
RULE(radius=1) [H+;H0:1].[H+;H0:2].[N;H0;+0:3]#[C;H0;+0:4]-[SH;+0:5].[OH2;+0:6]>>[NH3;+0:3].[O;H0;+0:6]=[C;H0;+0:4]=[S;H0;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Cloning of genes coding for the three subunits of thiocyanate hydrolase of Thiobacillus thioparus THI 115 and their evolutionary relationships to nitrile hydratase.Katayama Y, Matsushita Y, Kaneko M, Kondo M, Mizuno T, Nyunoya H1998 May9573140
Thiocyanate hydrolase, the primary enzyme initiating thiocyanate degradation in the novel obligately chemolithoautotrophic halophilic sulfur-oxidizing bacterium Thiohalophilus thiocyanoxidans.Bezsudnova EY, Sorokin DY, Tikhonova TV, Popov VO2007 Dec17964868
A thiocyanate hydrolase of Thiobacillus thioparus. A novel enzyme catalyzing the formation of carbonyl sulfide from thiocyanate.Katayama Y, Narahara Y, Inoue Y, Amano F, Kanagawa T, Kuraishi H1992 May 51577754