| 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 | ||||||||
| |||||||||
In enzymology, an acetylornithine deacetylase (EC 3.5.1.16) is an enzyme that catalyzes the chemical reaction
- 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[edit]
As 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.
