Biology:N-isopropylammelide isopropylaminohydrolase
| N-isopropylammelide isopropylaminohydrolase | |||||||||
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| Identifiers | |||||||||
| EC number | 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 | ||||||||
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In enzymology, a N-isopropylammelide isopropylaminohydrolase (EC 3.5.99.4) is an enzyme that catalyzes the chemical reaction
- N-isopropylammelide + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 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
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2QT3.
References
- "AtzC is a new member of the amidohydrolase protein superfamily and is homologous to other atrazine-metabolizing enzymes". J. Bacteriol. 180 (1): 152–8. 1998. doi:10.1128/JB.180.1.152-158.1998. PMID 9422605.
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