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In enzymology, an acetylornithine deacetylase (EC 3.5.1.16) is an enzyme that catalyzes the chemical reaction

N₂-acetyl-L-ornithine + H₂O ${\displaystyle \rightleftharpoons }$ 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

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2F7V and 2F8H.

References

• 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.

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