N-isopropylammelide isopropylaminohydrolase
| N-isopropylammelide isopropylaminohydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.99.4 | ||||||||
| 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 N-isopropylammelide isopropylaminohydrolase (EC 3.5.99.4) is an enzyme that catalyzes the chemical reaction
- N-isopropylammelide + H2O cyanuric acid + isopropylamine
Thus, the two substrates of this enzyme are N-isopropylammelide and H2O, whereas its two products are cyanuric acid and isopropylamine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is N-isopropylammelide isopropylaminohydrolase. This enzyme is also called AtzC. This enzyme participates in atrazine degradation.
Structural studies[edit]
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2QT3.
References[edit]
- Sadowsky MJ, Tong Z, de Souza M, Wackett LP (1998). "AtzC is a new member of the amidohydrolase protein superfamily and is homologous to other atrazine-metabolizing enzymes". J. Bacteriol. 180 (1): 152–8. doi:10.1128/JB.180.1.152-158.1998. PMC 106861. PMID 9422605.
