Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.104
Description:Cyanase.
Alternative Name: Cyanate lyase.
Cyanate hydrolase.
Cyanate hydratase.
Cyanate C-N-lyase.
Cyanate aminohydrolase.
Cath: 1.10.260.40; 3.30.1160.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.104
BRENDA Enzyme Link: BRENDA 4.2.1.104
KEGG Enzyme Link: KEGG4.2.1.104
BioCyc Enzyme Link: BioCyc 4.2.1.104
ExPASy Enzyme Link: ExPASy4.2.1.104
EC2PDB Enzyme Link: EC2PDB 4.2.1.104
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.104
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.104
IntEnz Enzyme Link: IntEnz 4.2.1.104
MEDLINE Enzyme Link: MEDLINE 4.2.1.104
MSA:

4.2.1.104;

Phylogenetic Tree:

4.2.1.104;

Uniprot:
M-CSA:
RHEA:11120 cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
RULE(radius=1) [*:1]=[C;H0;+0:2](-[OH;+0:3])-[OH;+0:4].[H+;H0:5].[H+;H0:6].[H+;H0:7].[N;H0;+0:8]#[C;H0;+0:9]-[OH;+0:10]>>[*:1]=[C;H0;+0:2]=[O;H0;+0:3].[NH3;+0:8].[O;H0;+0:4]=[C;H0;+0:9]=[O;H0;+0:10]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Reaction of the N-terminal methionine residues in cyanase with diethylpyrocarbonate.Anderson PM, Korte JJ, Holcomb TA1994 Nov 297947823
Role of bicarbonate/CO2 in the inhibition of Escherichia coli growth by cyanate.Kozliak EI, Fuchs JA, Guilloton MB, Anderson PM1995 Jun7768821
Purification and properties of the inducible enzyme cyanase.Anderson PM1980 Jun 246994799
Some properties of the induced enzyme cyanase.Taussig A1965 Jul5322950
Bicarbonate is a recycling substrate for cyanase.Johnson WV, Anderson PM1987 Jul 53110153
The synthesis of the induced enzyme, ''cyanase'', in E. coli.TAUSSIG A1960 Nov 1813775509
Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site.Walsh MA, Otwinowski Z, Perrakis A, Anderson PM, Joachimiak A2000 May 1510801492