The primary structure of ornithine aminotransferase. Identification of active-site sequence and site of post-translational proteolysis.
Tentative assignments of functional residues in rat liver mitochondrial ornithine aminotransferase have recently been made using the amino acid sequence deduced from a cDNA clone [(1985) J.Biol.Chem. 260, 12993-12997]. Partial sequences obtained using the pure mature protein demonstrate that one of these assignments, that of Lys 292 as the residue that binds the coenzyme pyridoxal phosphate, is correct. However, the identification of the Glu 34-Gln 35 bond as the site of post-translational proteolysis is in error. This cleavage occurs instead at Ala 25-Thr 26.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004247:DNA / Q000032:analysis; D008930:Mitochondria, Liver / Q000201:enzymology; D009953:Ornithine-Oxo-Acid Transaminase / Q000032:analysis*; D010455:Peptides / Q000032:analysis; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000032:analysis; D051381:Rats; D000637:Transaminases / Q000032:analysis*
D010455:Peptides; D021382:Protein Sorting Signals; D004247:DNA; D000637:Transaminases; D009953:Ornithine-Oxo-Acid Transaminase