title: Identity of beta-alanine-oxo-glutarate aminotransferase and L-beta-aminoisobutyrate aminotransferase in rat liver.
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.
mesh_terms: D000621:Aminoisobutyric Acids / Q000378:metabolism; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D007158:Immunologic Techniques; D008099:Liver / Q000201:enzymology*; D008297:Male; D051381:Rats; D013379:Substrate Specificity; D000637:Transaminases / Q000378:metabolism*; D015091:beta-Alanine / Q000378:metabolism
chemical_list: D000621:Aminoisobutyric Acids; D015091:beta-Alanine; D000637:Transaminases; C033435:3-aminoisobutyric acid