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Title: Identity of beta-alanine-oxo-glutarate aminotransferase and L-beta-aminoisobutyrate aminotransferase in rat liver. Author: Tamaki N, Fujimoto S, Mizota C, Kikugawa M. Journal: Biochim Biophys Acta; 1987 Aug 13; 925(2):238-40. PubMed ID: 3113494. Abstract: L-beta-Aminoisobutyrate served as an amino donor for purified beta-alanine-oxo-glutarate aminotransferase from rat liver when 2-oxoglutarate was employed as an amino acceptor, but the D-isomer did not. L-beta-Aminoisobutyrate acted as a competitive inhibitor with respect to beta-alanine and had a Ki of approximately 2.6 mM, which is the same value as the Km of 2.7 mM. When the crude extract was applied to a DEAE-Sepharose CL-6B column, L-beta-aminoisobutyrate aminotransferase and beta-alanine-oxo-glutarate aminotransferase activities were found in the same fractions with a single peak. Antiserum to rat liver beta-alanine-oxo-glutarate aminotransferase inhibited L-beta-aminoisobutyrate aminotransferase activity in rat liver in the same way as beta-alanine-oxo-glutarate aminotransferase activity.[Abstract] [Full Text] [Related] [New Search]