无色杆菌蛋白酶I对S-2-氨基乙基半胱氨酰肽键的水解作用。
Hydrolysis of S-2-aminoethylcysteinyl peptide bond by Achromobacter protease I.
作者信息
Masaki T, Takiya T, Tsunasawa S, Kuwahara S, Sakiyama F, Soejima M
机构信息
Department of Resource Biology, Faculty of Agriculture, Ibaraki University, Japan.
出版信息
Biosci Biotechnol Biochem. 1994 Jan;58(1):215-6. doi: 10.1271/bbb.58.215.
PMID:7764517
Abstract
The substrate specificity of Achromobacter protease I (API) was examined for S-2-aminoethyl(AE)cysteinyl bonds in Bz-AEC-OMe/OEt, Bz-AEC-NH2, and AE-insulin B chain. The protease hydrolyzed all of the tested AE-cysteinyl bonds at the same rate as that of lysyl bonds. Kinetic parameters were estimated for this hydrolysis reaction.
摘要
研究了无色杆菌蛋白酶I（API）对Bz-AEC-OMe/OEt、Bz-AEC-NH2和AE-胰岛素B链中S-2-氨基乙基（AE）半胱氨酰键的底物特异性。该蛋白酶以与赖氨酰键相同的速率水解所有测试的AE-半胱氨酰键。对该水解反应的动力学参数进行了估算。
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