The primary structure of ornithine aminotransferase. Identification of active-site sequence and site of post-translational proteolysis

FEBS Letters
M SimmacoF Bossa

Abstract

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.

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Citations

Oct 1, 1989·In Vitro Cellular & Developmental Biology : Journal of the Tissue Culture Association·J D Shull, H C Pitot
Oct 1, 1993·Molecular and Biochemical Parasitology·S R SchmidH A Stanley
Jan 18, 1989·Biochimica Et Biophysica Acta·F U HartlW Neupert
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Aug 3, 2010·Journal of Molecular Biology·Esther JortzikKatja Becker
Dec 16, 2016·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·Muthukumaran SivashanmugamSulochana K N
Oct 18, 2020·Biochimica Et Biophysica Acta. Proteins and Proteomics·Riccardo MontioliBarbara Cellini

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