EC number:3.5.3.9
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.3 In linear amidines |
| ID: | 3.5.3.9 |
|---|---|
| Description: | Allantoate deiminase. |
| Cath: | 3.30.70.360; 3.40.630.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.3.9 |
| BRENDA Enzyme Link: | BRENDA 3.5.3.9 |
| KEGG Enzyme Link: | KEGG3.5.3.9 |
| BioCyc Enzyme Link: | BioCyc 3.5.3.9 |
| ExPASy Enzyme Link: | ExPASy3.5.3.9 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.3.9 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.3.9 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.3.9 |
| IntEnz Enzyme Link: | IntEnz 3.5.3.9 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.3.9 |
| RHEA:27485 | allantoate + 2 H(+) + H2O = (S)-2-ureidoglycine + CO2 + NH4(+) |
| RULE(radius=1) | [*:1]-[NH;+0:2]-[C;H0;+0:3](=[*:4])-[NH2;+0:5].[H+;H0:6].[H+;H0:7].[OH2;+0:8]>>[*:1]-[NH2;+0:2].[*:4]=[C;H0;+0:3]=[O;H0;+0:8].[NH3;+0:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Reversible activation of allantoate amidohydrolase by acid-pretreatment and other properties of the enzyme. | Vogels GD | 1966 Feb 14 | 5328936 |
| Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria. | Serventi F, Ramazzina I, Lamberto I, Puggioni V, Gatti R, Percudani R | 2010 Feb 19 | 20038185 |