Kline E L, Manross D N, Warwick M L
J Bacteriol. 1977 May;130(2):951-3. doi: 10.1128/jb.130.2.951-953.1977.
In a strain of Escherichia coli K-12 lacking threonine deaminase, the enzyme converting alpha-ketoisovalerate and alpha-keto-beta-methylvalerate to valine and isoleucine, respectively, was multivalently repressed by valine, isoleucine, and leucine. This activity was due to transaminase B, specified by the ilvE structural gene.
在一株缺乏苏氨酸脱氨酶的大肠杆菌K-12中,分别将α-酮异戊酸和α-酮-β-甲基戊酸转化为缬氨酸和异亮氨酸的酶受到缬氨酸、异亮氨酸和亮氨酸的多价阻遏。这种活性归因于转氨酶B,它由ilvE结构基因所编码。