EC Tree |
3. Hydrolases |
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
3.5.5 In nitriles |
ID: | 3.5.5.2 |
---|---|
Description: | Ricinine nitrilase. |
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 3.5.5.2 |
BRENDA Enzyme Link: | BRENDA 3.5.5.2 |
KEGG Enzyme Link: | KEGG3.5.5.2 |
BioCyc Enzyme Link: | BioCyc 3.5.5.2 |
ExPASy Enzyme Link: | ExPASy3.5.5.2 |
EC2PDB Enzyme Link: | EC2PDB 3.5.5.2 |
ExplorEnz Enzyme Link: | ExplorEnz 3.5.5.2 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.5.5.2 |
IntEnz Enzyme Link: | IntEnz 3.5.5.2 |
MEDLINE Enzyme Link: | MEDLINE 3.5.5.2 |
RHEA:22704 | 2 H2O + ricinine = 4-methoxy-1-methyl-2-oxo-1,2-dihydropyridine-3-carboxylate + NH4(+) |
RULE(radius=1) | [*:1]-[C;H0;+0:2]#[N;H0;+0:3].[OH2;+0:4].[OH2;+0:5]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:5])-[OH;+0:4].[NH3;+0:3] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
RICININE NITRILASE. II. PURIFICATION AND PROPERTIES. | HOOK RH, ROBINSON WG | 1964 Dec | 14247680 |
RICININE NITRILASE. I. REACTION PRODUCT AND SUBSTRATE SPECIFICITY. | ROBINSON WG, HOOK RH | 1964 Dec | 14247679 |
The nitrilase superfamily: classification, structure and function. | Pace HC, Brenner C | 2001 | 11380987 |