| biuret amidohydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.84 | ||||||||
| 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 | ||||||||
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In enzymology, a biuret amidohydrolase (EC 3.5.1.84) is an enzyme that catalyzes the chemical reaction
- biuret + H2O urea(CH4N2O) + CO2 + NH3
urea(CH4N2O) + CO2 + NH3Thus, the two substrates of this enzyme are biuret and H2O, whereas its 3 products are urea, CO2, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is biuret amidohydrolase. This enzyme participates in atrazine degradation.
References
- Cook AM, Beilstein P, Grossenbacher H, Hutter R (1985). "Ring cleavage and degradative pathway of cyanuric acid in bacteria". Biochem. J. 231 (1): 25–30. PMC 1152698. PMID 3904735.
| 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 | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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