Involvement of L-tryptophan aminotransferase in indole-3-acetic acid biosynthesis in Enterobacter cloacae.

@article{Koga1994InvolvementOL,
  title={Involvement of L-tryptophan aminotransferase in indole-3-acetic acid biosynthesis in Enterobacter cloacae.},
  author={Jinichiro Koga and Kunihiko Syōno and Teruo Ichikawa and Takahiro Adachi},
  journal={Biochimica et biophysica acta},
  year={1994},
  volume={1209 2},
  pages={241-7}
}
L-Tryptophan aminotransferase (L-tryptophan:2-oxoglutarate aminotransferase; EC 2.6.1.27) from Enterobacter cloacae was purified 62-fold and characterized to determine its role in indole-3-acetic acid biosynthesis. The enzyme reversibly catalyzed the transamination of L-tryptophan with 2-oxoglutarate as the amino acceptor to yield indole-3-pyruvic acid and L-glutamate, and the Km values for L-tryptophan and indole-3-pyruvic acid were 3.3 mM and 24 microM, respectively. In the indole-3… CONTINUE READING
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