Acetylornithine transaminase

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

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

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.

Reaction

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]

Alternative Names

Several alternative names are used for acetylornithine transaminase, including:

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

Structural Information

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

References

↑ Albrecht, Alberta M.; Vogel, Henry J. (1964-06). "Acetylornithine δ-Transaminase". Journal of Biological Chemistry. 239 (6): 1872–1876. doi:10.1016/s0021-9258(18)91275-5. ISSN 0021-9258. {{cite journal}}: Check date values in: |date= (help)

[1] Albrecht, Alberta M.; Vogel, Henry J. (1964-06). "Acetylornithine δ-Transaminase". Journal of Biological Chemistry. 239 (6): 1872–1876. doi:10.1016/s0021-9258(18)91275-5. ISSN 0021-9258. {{cite journal}}: Check date values in: |date= (help)

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