大肠杆菌K12天冬氨酸激酶I-高丝氨酸脱氢酶I的一级结构。枯草杆菌蛋白酶有限蛋白水解切割位点。
The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Site of limited proteolytic cleavage by subtilisin.
作者信息
Briley P A, Sibilli L, Chalvignac M A, Cossart P, Le Bras G, De Wolf A, Cohen G N
出版信息
J Biol Chem. 1978 Dec 25;253(24):8867-71.
PMID:363710
Abstract
The sequence of the first 25 residues of the homoserine dehydrogenase fragment, produced by limited proteolysis of aspartokinase I-homoserine dehydrogenase I with substilisin, has been determined. The sequence of a cyanogen bromide peptide (CB5, 59 residues), isolated from the entire protein, is also presented. Residues 1 to 18 of the subtilisin homoserine dehydrogenase fragment match the sequence 42 to 59 of peptide CB5.
摘要
已确定用枯草杆菌蛋白酶对天冬氨酸激酶I-高丝氨酸脱氢酶I进行有限蛋白酶解所产生的高丝氨酸脱氢酶片段前25个残基的序列。还给出了从完整蛋白质中分离出的溴化氰肽（CB5，59个残基）的序列。枯草杆菌蛋白酶高丝氨酸脱氢酶片段的第1至18个残基与肽CB5的第42至59个序列匹配。
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