Identity of D-3-aminoisobutyrate-pyruvate aminotransferase with alanine-glyoxylate aminotransferase 2.

@article{Kontani1993IdentityOD,
  title={Identity of D-3-aminoisobutyrate-pyruvate aminotransferase with alanine-glyoxylate aminotransferase 2.},
  author={Yukari Kontani and Masaharu Kaneko and M Kikugawa and Sadaki Fujimoto and Nanaya Tamaki},
  journal={Biochimica et biophysica acta},
  year={1993},
  volume={1156 2},
  pages={161-6}
}
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… CONTINUE READING

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