Allophanate hydrolase
| allophanate hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.54 | ||||||||
| CAS number | 79121-96-3 | ||||||||
| 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 / EGO | ||||||||
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In enzymology, an allophanate hydrolase (EC 3.5.1.54) is an enzyme that catalyzes the chemical reaction
- allophanate + 3 H2O + H+
2 HCO3− + 2 NH4+
Thus, the two substrates of this enzyme are allophanate (urea-1-carboxylate or N-carbamoylcarbamate) and H2O, whereas its two products are HCO3− and NH4+.
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 urea-1-carboxylate amidohydrolase. This enzyme is also called allophanate lyase. This enzyme participates in urea cycle and metabolism of amino groups and atrazine degradation.
See also
References
- Maitz GS, Haas EM and Castric PA (1982). "Purification and properties of the allophanate hydrolase from Chlamydomonas reinhardii". Biochim. Biophys. Acta 714: 486–491. doi:10.1016/0304-4165(82)90158-1.
- Roon RJ, Levenberg B (1972). "Urea amidolyase. I. Properties of the enzyme from Candida utilis". J. Biol. Chem. 247 (13): 4107–13. PMID 4556303.
- Sumrada RA, Cooper TG (1982). "Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast". J. Biol. Chem. 257 (15): 9119–27. PMID 6124544.
- Kanamori T, Kanou N, Kusakabe S, Atomi H, Imanaka T (2005). "Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea". FEMS. Microbiol. Lett. 245 (1): 61–5. doi:10.1016/j.femsle.2005.02.023. PMID 15796980.