Jany K D, Bekelar K, Pfleiderer G, Ishay J
Biochem Biophys Res Commun. 1983 Jan 14;110(1):1-7. doi: 10.1016/0006-291x(83)91251-2.
The complete amino acid sequence of the endopeptidase II from the larvae of the hornet, Vespa orientalis, has been determined. The enzyme is a single polypeptide chain of 216 residues. The protease is a serine endopeptidase. When aligned for optimal homology to the trypsin related proteases, the insect endopeptidase displays 37% identity with bovine chymotrypsin. The structure of the hornet protease is the first reported for a serine endopeptidase from an insect.
已确定东方胡蜂幼虫的内肽酶II的完整氨基酸序列。该酶是一条由216个残基组成的单多肽链。该蛋白酶是一种丝氨酸内肽酶。当与胰蛋白酶相关蛋白酶进行最佳同源性比对时,这种昆虫内肽酶与牛胰凝乳蛋白酶的同源性为37%。胡蜂蛋白酶的结构是首次报道的来自昆虫的丝氨酸内肽酶的结构。