Drapeau G R
Can J Biochem. 1978 Jun;56(6):534-44. doi: 10.1139/o78-082.
The amino acid sequence of staphylococcal protease has been determined by analysis of tryptic peptides obtained from cyanogen bromide fragments. Selected peptides obtained from digests with staphylococcal protease, thermolysin, and chymotrypsin provided the information necessary to align the tryptic peptides and the cyanogen bromide fragments. The protease is a single polypeptide chain of some 250 amino acids and is devoid of sulfhydryl groups. The COOH-terminal tryptic peptide of of the protease molecule contains some 43 residues, most of which are aspartic acids, asparagines, and prolines. The amino acid sequence of this peptide was not determined. The primary structure near the active serine residue indicates that staphylococcal protease is related to the pancreatic serine proteases. However, it has little or no additional sequence homologies with these enzymes except for the regions near histidine-50 and aspartic acid - 91. These regions have striking similarities with the corresponding regions of protease B and the trypsin-like enzyme of Streptomyces griseus.
通过对从溴化氰片段获得的胰蛋白酶肽段进行分析，已确定葡萄球菌蛋白酶的氨基酸序列。从用葡萄球菌蛋白酶、嗜热菌蛋白酶和胰凝乳蛋白酶消化得到的选定肽段，提供了排列胰蛋白酶肽段和溴化氰片段所需的信息。该蛋白酶是一条约含250个氨基酸的单多肽链，且不含巯基。蛋白酶分子的羧基末端胰蛋白酶肽段含有约43个残基，其中大部分是天冬氨酸、天冬酰胺和脯氨酸。该肽段的氨基酸序列未确定。活性丝氨酸残基附近的一级结构表明，葡萄球菌蛋白酶与胰腺丝氨酸蛋白酶相关。然而，除了组氨酸-50和天冬氨酸-91附近的区域外，它与这些酶几乎没有或没有额外的序列同源性。这些区域与蛋白酶B和灰色链霉菌的胰蛋白酶样酶的相应区域有显著相似性。
