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.