Fried V A
J Bacteriol. 1980 Jul;143(1):506-9. doi: 10.1128/jb.143.1.506-509.1980.
The lac thiogalactoside transacetylase was purified from both a wild-type Escherichia coli K-12 strain (H3000) and an E. coli ML strain (ML308). These enzymes are indistinguishable by using several criteria. The subunit molecular weight of the enzyme is 24,800, which is significantly less than the previously reported value of 30,000. Although the function of the thiogalactoside transacetylase is unknown, it is suggested that this enzyme plays an important role in lactose utilization since its structure and enzymatic activity have been conserved.
硫代半乳糖苷转乙酰酶是从野生型大肠杆菌K-12菌株(H3000)和大肠杆菌ML菌株(ML308)中纯化得到的。通过几种标准判断,这些酶无法区分。该酶的亚基分子量为24,800,明显低于先前报道的30,000这一数值。尽管硫代半乳糖苷转乙酰酶的功能尚不清楚,但由于其结构和酶活性得到了保留,推测该酶在乳糖利用中发挥着重要作用。