Purification and characterization of l-alanine: 4,5-dioxovalerate (glyoxylate) aminotransferase from radish (raphanus sativus l.) seedlings

Yuzo Shioi, Michio Doi, Tsutomu Sasa

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L-Alanine:4,5-dioxovalerate (DOVA) aminotransferase was purified 131-fold and characterized from greening seedlings of radish (Raphanus sativus L.). The enzyme was shown to be identical with alanine:glyoxylate aminotransferase. The rate of activity of DOVA aminotransferase was 15 times less than that of glyoxylate aminotransferase. Its molecular weight was estimated to be approximately 123,000 with two identical subunits, and exhibited a single, broad pH optimum at 8.0. DOVA aminotransferase activity was competitively inhibited by glyoxylate. A kinetic study of the enzyme at different alanine concentrations suggested a ping pong reaction mechanism. The Km values for DOVA and L-alanine were 0.71 and 1.7 mM, respectively.The activity ratio of transamination under various conditions, the cellular localization of the enzyme and the lack of correlation between the activity of this enzyme and chlorophyll synthesis, indicate that DOVA aminotransferase in radish is not involved in 5-aminolevulinate synthesis.

Original languageEnglish
Pages (from-to)1487-1493
Number of pages7
JournalPlant and Cell Physiology
Issue number8
Publication statusPublished - Jan 1 1984


All Science Journal Classification (ASJC) codes

  • Physiology
  • Plant Science
  • Cell Biology

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