Purification and properties of branched chain amino acid aminotransferase from gramicidin S-producing Bacillus brevis.

@article{Kanda1995PurificationAP,
  title={Purification and properties of branched chain amino acid aminotransferase from gramicidin S-producing Bacillus brevis.},
  author={Mina Kanda and Kazuyuki Hori and Takuzo Kurotsu and K Ohgishi and Takehisa Hanawa and Yohtaro Saito},
  journal={Journal of nutritional science and vitaminology},
  year={1995},
  volume={41 1},
  pages={51-60}
}
The branched chain amino acid aminotransferase [EC 2.6.1.42] was purified to a homogeneous state from a gramicidin S-producing strain of Bacillus brevis. The enzyme had a molecular weight of about 93,000 and consisted of two identical subunits, each with a molecular weight of about 47,000. One pyridoxal phosphate is bound per subunit. In addition to branched chain amino acids, the enzyme uses L-phenylalanine and L-tryptophan as the amino donor, indicating that B. brevis branched chain amino… CONTINUE READING