EC number:3.5.3.26
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.3 In linear amidines |
| ID: | 3.5.3.26 |
|---|---|
| Description: | (S)-ureidoglycine aminohydrolase. |
| Cath: | 2.60.120.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.3.26 |
| BRENDA Enzyme Link: | BRENDA 3.5.3.26 |
| KEGG Enzyme Link: | KEGG3.5.3.26 |
| BioCyc Enzyme Link: | BioCyc 3.5.3.26 |
| ExPASy Enzyme Link: | ExPASy3.5.3.26 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.3.26 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.3.26 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.3.26 |
| IntEnz Enzyme Link: | IntEnz 3.5.3.26 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.3.26 |
| RHEA:25241 | (S)-2-ureidoglycine + H2O = (S)-ureidoglycolate + NH4(+) |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[OH2;+0:5]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:5].[NH3;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics. | Agarwal R, Burley SK, Swaminathan S | 2007 Apr 27 | 17362992 |