Kanda M, Hori K, Kurotsu T, Ohgishi K, Hanawa T, Saito Y
Department of Biochemistry, Hyogo College of Medicine, Nishinomiya, Japan.
J Nutr Sci Vitaminol (Tokyo). 1995 Feb;41(1):51-60. doi: 10.3177/jnsv.41.51.
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.
从短芽孢杆菌的一个产短杆菌肽S的菌株中，将支链氨基酸转氨酶[EC 2.6.1.42]纯化至均一状态。该酶的分子量约为93,000，由两个相同的亚基组成，每个亚基的分子量约为47,000。每个亚基结合一个磷酸吡哆醛。除支链氨基酸外，该酶还使用L-苯丙氨酸和L-色氨酸作为氨基供体，这表明短芽孢杆菌支链氨基酸转氨酶对氨基供体具有广泛的底物特异性。该酶利用2-氧代戊二酸作为氨基受体。纯化后的酶在中性pH条件下，在332和427 nm处呈现吸收最大值。
