In enzymology, an acetylornithine deacetylase (EC 3.5.1.16) is an enzyme that catalyzes the chemical reaction
| acetylornithine deacetylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.16 | ||||||||
| CAS no. | 9025-12-1 | ||||||||
| 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 | ||||||||
| |||||||||
- N2-acetyl-L-ornithine + H2O acetate + L-ornithine
Thus, the two substrates of this enzyme are N2-acetyl-L-ornithine and H2O, whereas its two products are acetate and L-ornithine.
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 N2-acetyl-L-ornithine amidohydrolase. Other names in common use include acetylornithinase, N-acetylornithinase, and 2-N-acetyl-L-ornithine amidohydrolase. This enzyme participates in urea cycle and metabolism of amino groups.
Structural studies
editAs of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2F7V and 2F8H.
References
edit- Vogel HJ (1953). "Path of Ornithine Synthesis in Escherichia Coli". Proc. Natl. Acad. Sci. U.S.A. 39 (7): 578–83. Bibcode:1953PNAS...39..578V. doi:10.1073/pnas.39.7.578. PMC 1063827. PMID 16589307.
- VOGEL HJ, BONNER DM (1956). "Acetylornithinase of Escherichia coli: partial purification and some properties". J. Biol. Chem. 218 (1): 97–106. doi:10.1016/S0021-9258(18)65874-0. PMID 13278318.
