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  • 标题:Purification and Properties of Branched Chain Amino Acid Aminotransferase from Gramicidin S-Producing Bacillus brevis
  • 本地全文:下载
  • 作者:Masayuki KANDA ; Kazuko HORI ; Toshitsugu KUROTSU
  • 期刊名称:Journal of Nutritional Science and Vitaminology
  • 印刷版ISSN:0301-4800
  • 电子版ISSN:1881-7742
  • 出版年度:1995
  • 卷号:41
  • 期号:1
  • 页码:51-60
  • DOI:10.3177/jnsv.41.51
  • 出版社:Center for Academic Publications Japan
  • 摘要: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 acid aminotransferase has a broad substrate specificity for the amino donor. The enzyme utilized 2-oxoglutarate as the amino acceptor. The purified enzyme exhibits its absorption maxima at 332 and 427 nm at neutral pH.
  • 关键词:branched chain amino acid aminotransferase;Bacillus brevis;Gramicidin S;pyridoxal phosphate
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