The Enzyme Database

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EC 2.6.1.11     
Accepted name: acetylornithine transaminase
Reaction: N2-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
For diagram of ornithine biosynthesis, click here
Other name(s): acetylornithine δ-transaminase; ACOAT; acetylornithine 5-aminotransferase; acetylornithine aminotransferase; N-acetylornithine aminotransferase; N-acetylornithine-δ-transaminase; N2-acetylornithine 5-transaminase; N2-acetyl-L-ornithine:2-oxoglutarate aminotransferase; succinylornithine aminotransferase; 2-N-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase
Systematic name: N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on L-ornithine and N2-succinyl-L-ornithine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-40-4
References:
1.  Albrecht, A. and Vogel, H.J. Acetylornithine δ-transaminase. Partial purification and repression behavior. J. Biol. Chem. 239 (1964) 1872–1876. [PMID: 14213368]
2.  Vogel, H.J. Path of ornithine synthesis in Escherichia coli. Proc. Natl. Acad. Sci. USA 39 (1953) 578–583. [PMID: 16589307]
3.  Vander Wauven, C. and Stalon, V. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. J. Bacteriol. 164 (1985) 882–886. [PMID: 2865249]
4.  Voellmy, R. and Leisinger, T. Dual role for N-2-acetylornithine 5-aminotransferase from Pseudomonas aeruginosa in arginine biosynthesis and arginine catabolism. J. Bacteriol. 122 (1975) 799–809. [PMID: 238949]
[EC 2.6.1.11 created 1961, modified 2004 (EC 2.6.1.69 created 1989, incorporated 2004)]
 
 


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