来自大肠杆菌K12的甲硫氨酸可抑制天冬氨酸激酶II - 高丝氨酸脱氢酶II的亚基结构。
Subunit structure of the methionine-repressible aspartokinase II--homoserine dehydrogenase II from Escherichia coli K12.
作者信息
Dautry-Varsat A, Sibilli-Weill L, Cohen G N
出版信息
Eur J Biochem. 1977 Jun 1;76(1):1-6. doi: 10.1111/j.1432-1033.1977.tb11563.x.
The quaternary structure of Escherichia coli K12 aspartokinase II--homoserine dehydrogenase II has been examined. This multifunctional protein has a molecular weight Mr = 176000. It is composed of two subunits having the same molecular weight and the same charge. The results obtained from the examination of tryptic maps, the number and amino acid composition of cysteine-containing peptides and the uniqueness of the N-terminal sequence, strongly suggest that the 2 subunits are identical. The properties of aspartokinase II--homoserine dehydrogenase II can be compared to those of the much better known protein aspartokinase I--homoserine dehydrogenase I.
对大肠杆菌K12天冬氨酸激酶II-高丝氨酸脱氢酶II的四级结构进行了研究。这种多功能蛋白质的分子量Mr = 176000。它由两个分子量和电荷相同的亚基组成。通过胰蛋白酶图谱分析、含半胱氨酸肽段的数量和氨基酸组成以及N端序列的独特性所获得的结果，强烈表明这两个亚基是相同的。天冬氨酸激酶II-高丝氨酸脱氢酶II的性质可以与更为人熟知的蛋白质天冬氨酸激酶I-高丝氨酸脱氢酶I的性质进行比较。
Zotero 插件