Acetylornithine transaminase

In enzymology, an acetylornithine transaminase (EC 2.6.1.11) is an enzyme that catalyzes the chemical reaction

N2-acetyl-L-ornithine + 2-oxoglutarate N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
acetylornithine transaminase
Identifiers
EC number2.6.1.11
CAS number9030-40-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are N2-acetyl-L-ornithine and 2-oxoglutarate, whereas its two products are N-acetyl-L-glutamate 5-semialdehyde and L-glutamate.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase. Other names in common use include acetylornithine delta-transaminase, ACOAT, acetylornithine 5-aminotransferase, acetylornithine aminotransferase, N-acetylornithine aminotransferase, N-acetylornithine-delta-transaminase, N2-acetylornithine 5-transaminase, N2-acetyl-L-ornithine:2-oxoglutarate aminotransferase, succinylornithine aminotransferase, and 2-N-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase. This enzyme participates in urea cycle and metabolism of amino groups. It employs one cofactor, pyridoxal phosphate.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1VEF, 1WKG, 1WKH, 2E54, 2EH6, and 2ORD.

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References
    • ALBRECHT AM, VOGEL HJ (1964). "ACETYLORNITHINE DELTA-TRANSAMINASE. PARTIAL PURIFICATION AND REPRESSION BEHAVIOR". J. Biol. Chem. 239: 1872–6. PMID 14213368.
    • Vogel HJ (1953). "Path of Ornithine Synthesis in Escherichia Coli". Proc. Natl. Acad. Sci. U.S.A. 39 (7): 578–83. doi:10.1073/pnas.39.7.578. PMC 1063827. PMID 16589307.
    • Voellmy R, Leisinger T (1975). "Dual role for N-2-acetylornithine 5-aminotransferase from Pseudomonas aeruginosa in arginine biosynthesis and arginine catabolism". J. Bacteriol. 122 (3): 799–809. PMC 246128. PMID 238949.


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