Purification and Properties of Branched Chain Amino Acid Aminotransferase from Gramicidin S-Producing Bacillus brevis.
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概要
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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.
- 財団法人 学会誌刊行センターの論文
著者
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KANDA Masayuki
Department of Biochemistry, Hyogo College of Medicine
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Hori Kazuko
Department Of Biochemistry Hyogo College Of Medicine
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Kanda Masayuki
Department Of Biochemistry Hyogo College Of Medicine
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Hanawa Tomoko
Department Of Infectious Diseases Kyorin University School Of Medicine
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Saito Yoshitaka
Department Of Biochemistry Hyogo College Of Medicine
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Kurotsu Toshitsugu
Department Of Biochemistry Hyogo College Of Medicine
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SAITO YOSHITAKA
Department of Biochemistry, Hyogo College of Medicine
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OHGISHI Katsuko
Department of Biochemistry, Hyogo College of Medicine
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HANAWA Tomoko
Department of Biochemistry, Hyogo College of Medicine
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