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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.
PMID: 3754226 [PubMed - indexed for MEDLINE]
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Cited by 6 PubMed Central articles
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Pyridoxine-responsive gyrate atrophy of the choroid and retina: clinical and biochemical correlates of the mutation A226V.
Michaud J, Thompson GN, Brody LC, Steel G, Obie C, Fontaine G, Schappert K, Keith CG, Valle D, Mitchell GA.
Am J Hum Genet. 1995 Mar; 56(3):616-22.
[Am J Hum Genet. 1995]
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Molecular basis of ornithine aminotransferase deficiency in B-6-responsive and -nonresponsive forms of gyrate atrophy.
Ramesh V, McClatchey AI, Ramesh N, Benoit LA, Berson EL, Shih VE, Gusella JF.
Proc Natl Acad Sci U S A. 1988 Jun; 85(11):3777-80.
[Proc Natl Acad Sci U S A. 1988]
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An initiator codon mutation in ornithine-delta-aminotransferase causing gyrate atrophy of the choroid and retina.
Mitchell GA, Brody LC, Looney J, Steel G, Suchanek M, Dowling C, Der Kaloustian V, Kaiser-Kupfer M, Valle D.
J Clin Invest. 1988 Feb; 81(2):630-3.
[J Clin Invest. 1988]
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