Acetylornithine deacetylase
From Wikipedia, the free encyclopedia
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.
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[edit] Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2F7V and 2F8H.
[edit] References
- IUBMB entry for 3.5.1.16
- BRENDA references for 3.5.1.16 (Recommended.)
- PubMed references for 3.5.1.16
- PubMed Central references for 3.5.1.16
- Google Scholar references for 3.5.1.16
- Vogel HJ (1953). "Path of Ornithine Synthesis in Escherichia Coli". Proc. Natl. Acad. Sci. U. S. A. 39: 578–83. doi:. PMID 16589307.
- VOGEL HJ, BONNER DM (1956). "Acetylornithinase of Escherichia coli: partial purification and some properties". J. Biol. Chem. 218: 97–106. PMID 13278318.
[edit] External links
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- The CAS registry number for this enzyme class is 9025-12-1.

