Crystal Data for a Bacterial Serine Protease
Crystal Data for a Bacterial Serine Protease
复制标题
细菌丝氨酸蛋白酶的水晶数据
作者：
M. James;L. Smillie
α-LYTIC 蛋白酶是从土壤芽孢杆菌 Sorangium sp 的培养滤液中分离出来的几种蛋白水解酶之一。 （粘杆菌405）1。该酶的化学和动力学研究表明，它与胰丝氨酸蛋白酶胰凝乳蛋白酶 A 和 B、胰蛋白酶和弹性蛋白酶有许多显着的同源性。例如，α-裂解蛋白酶在活性丝氨酸周围具有与胰酶 1,2 完全相同的序列 (.Gly.Asp.Ser*.Gly.Gly.)。此外，酶 (Val.Thr.Ala.Gly.His.Cys.Gly.)3 中单个组氨酸残基周围的序列与胰凝乳蛋白酶 A4,5 和 B6 的 His 57 周围的序列以及胰蛋白酶7,8 和胰腺弹性蛋白酶9 的相应组氨酸残基周围的相似序列非常匹配。
α-LYTIC protease is one of several proteolytic enzymes isolated from culture filtrates of a soil bacillus Sorangium sp. (Myxobacter 405)1. Chemical and kinetic studies of this enzyme have shown many remarkable homologies with the pancreatic serine proteases chymotrypsins A and B, trypsin and elastase. For example, α-lytic protease has exactly the same sequence (.Gly.Asp.Ser*.Gly.Gly.) around the active serine as have the pancreatic enzymes1,2. Moreover, the sequence around the single histidine residue in the enzyme (Val.Thr.Ala.Gly.His.Cys.Gly.)3 closely matches the sequence around His 57 of chymotrypsins A4,5 and B6, and the similar sequences around the corresponding histidine residues of trypsin7,8 and pancreatic elastase9.