Acetylornithine transaminase

This article uses too much jargon, which needs explaining or simplifying. Please help improve the page to make it understandable for everybody, without removing the technical details. (September 2024)

Acetylornithine transaminase (EC 2.6.1.11) is an enzyme that catalyzes the reaction:

${\displaystyle N2-acetyl-L-ornithine+2-oxoglutarate\rightleftharpoons N-acetyl-L-glutamate5-semialdehyde+L-glutamate}$

This reaction plays a crucial role in the urea cycle and amino acid metabolism by transferring nitrogenous groups. The enzyme belongs to the family of transferases, specifically the transaminases. It requires the cofactor pyridoxal phosphate to function.

The enzyme's substrates are N2-acetyl-L-ornithine and 2-oxoglutarate, and its products are N-acetyl-L-glutamate 5-semialdehyde and L-glutamate.^[1]

Several alternative names are used for acetylornithine transaminase, including:

• Acetylornithine delta-transaminase
• ACOAT
• Acetylornithine 5-aminotransferase
• N-acetylornithine-delta-transaminase
• Succinylornithine aminotransferase

As of 2007, six structures have been solved for this enzyme class, with PDB accession codes: 1VEF, 1WKG, 1WKH, 2E54, 2EH6, and 2ORD.