| cyanuric acid amidohydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.2.15 | ||||||||
| CAS no. | 100785-00-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a cyanuric acid amidohydrolase (EC 3.5.2.15) is an enzyme that catalyzes the chemical reaction
- cyanuric acid + H2O biuret + CO2
biuret + CO2Thus, the two substrates of this enzyme are cyanuric acid and H2O, whereas its two products are biuret and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is cyanuric acid amidohydrolase. This enzyme participates in atrazine degradation.
References
- Eaton RW, Karns JS (1991). "Cloning and comparison of the DNA encoding ammelide aminohydrolase and cyanuric acid amidohydrolase from three s-triazine-degrading bacterial strains". J. Bacteriol. 173 (3): 1363–6. PMC 207267. PMID 1991731.
- Eaton RW, Karns JS (1991). "Cloning and analysis of s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227". J. Bacteriol. 173 (3): 1215–22. PMC 207245. PMID 1846859.
| Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
|---|---|
| 3.5.1: Linear amides / Amidohydrolases | |
| 3.5.2: Cyclic amides/ Amidohydrolases | |
| 3.5.3: Linear amidines/ Ureohydrolases | |
| 3.5.4: Cyclic amidines/ Aminohydrolases | |
| 3.5.5: Nitriles/ Aminohydrolases | |
| 3.5.99: Other | |
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
|
This EC 3.5 enzyme-related article is a stub. You can help Misplaced Pages by expanding it. |