EC number:3.5.2.15
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.2 In cyclic amides |
| ID: | 3.5.2.15 |
|---|---|
| Description: | Cyanuric acid amidohydrolase. |
| Cath: | 3.10.490.10; 3.30.1330.160; 3.30.1330.170; 3.30.1330.180; 3.30.1360.40; 3.90.1300.10; 1.20.58.1700; 2.40.100.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.2.15 |
| BRENDA Enzyme Link: | BRENDA 3.5.2.15 |
| KEGG Enzyme Link: | KEGG3.5.2.15 |
| BioCyc Enzyme Link: | BioCyc 3.5.2.15 |
| ExPASy Enzyme Link: | ExPASy3.5.2.15 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.2.15 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.2.15 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.2.15 |
| IntEnz Enzyme Link: | IntEnz 3.5.2.15 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.2.15 |
| RHEA:14641 | cyanurate + H2O = biuret + CO2 |
| RULE(radius=1) | [OH2;+0:1].[OH;+0:2]-[c;H0;+0:3]1:[n;H0;+0:4]:[c;H0;+0:5](-[OH;+0:6]):[n;H0;+0:7]:[c;H0;+0:8](-[OH;+0:9]):[n;H0;+0:10]:1>>[NH2;+0:4]-[C;H0;+0:3](=[O;H0;+0:2])-[NH;+0:10]-[C;H0;+0:8](-[NH2;+0:7])=[O;H0;+0:9].[O;H0;+0:1]=[C;H0;+0:5]=[O;H0;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| On the origins of cyanuric acid hydrolase: purification, substrates, and prevalence of AtzD from Pseudomonas sp. strain ADP. | Fruchey I, Shapir N, Sadowsky MJ, Wackett LP | 2003 Jun | 12788776 |
| Complete nucleotide sequence and organization of the atrazine catabolic plasmid pADP-1 from Pseudomonas sp. strain ADP. | Martinez B, Tomkins J, Wackett LP, Wing R, Sadowsky MJ | 2001 Oct | 11544232 |