Identity of D-3-aminoisobutyrate-pyruvate aminotransferase with alanine-glyoxylate aminotransferase 2. 
D-3-Aminoisobutyrate-pyruvate aminotransferase (EC 2.6.1.40) and alanine-glyoxylate aminotransferase 2 (EC 2.6.1.44) were co-purified from rat liver as a single protein.  The ratio of the two activities remained constant after Sephacryl S-200 chromatography and chromatofocussing.  The Km value for beta-alanine as a substrate with 1 mM glyloxylate as amino group acceptor was 1.4 mM. The activity was inhibited by (S)-alanine with Ki = 2.2 mM. The Km for (S)-alanine as substrate with 1 mM glyoxylate as amino group was 6 mM. This activity was inhibited competitively by beta-alanine with Ki = 0.7 mM. (R)-3-aminoisobutyric acid, 5-aminolevulinic acid, NG,NG'-dimethyl-(S)-arginine, and (S)-2-aminobutyric acid were active competitively with respect to beta-alanine with Km of 0.12 mM, 2.1 mM, 6.4 mM and 11.3 mM, respectively.  Antiserum to rat liver D-3-aminoisobutyrate-pyruvate aminotransferase inhibited alanine-glyoxylate aminotransferase activity in rat liver in the same way as that of D-3-aminoisobutyrate-pyruvate aminotransferase.  Alanine-glyoxylate aminotransferase activity and D-3-aminoisobutyrate-pyruvate aminotransferase activities were inactivated competitively with respect to beta-alanine by 5-fluorouracil and 6-azauracil, which are chemotherapeutic reagents used to cancer.  These experiments indicate that D-3-aminoisobutyrate-pyruvate aminotransferase is identical with alanine-glyoxylate aminotransferase 2, aminolevulinate aminotransferase, 2-aminobutyrate aminotransferase and dimetylarginine-pyruvate aminotransferase.