| 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; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| 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: | |
|---|---|
| Phylogenetic Tree: | |
| 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Reaction of the N-terminal methionine residues in cyanase with diethylpyrocarbonate. | Anderson PM, Korte JJ, Holcomb TA | 1994 Nov 29 | 7947823 |
| Role of bicarbonate/CO2 in the inhibition of Escherichia coli growth by cyanate. | Kozliak EI, Fuchs JA, Guilloton MB, Anderson PM | 1995 Jun | 7768821 |
| Purification and properties of the inducible enzyme cyanase. | Anderson PM | 1980 Jun 24 | 6994799 |
| Some properties of the induced enzyme cyanase. | Taussig A | 1965 Jul | 5322950 |
| Bicarbonate is a recycling substrate for cyanase. | Johnson WV, Anderson PM | 1987 Jul 5 | 3110153 |
| The synthesis of the induced enzyme, ''cyanase'', in E. coli. | TAUSSIG A | 1960 Nov 18 | 13775509 |
| 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 A | 2000 May 15 | 10801492 |