摘要
脱卤酶是催化α-卤酸转化为α-羟基酸的酶。本文用各种化学修饰剂对脱卤酶YL、109和H-2进行化学修饰。实验结果表明作用于丝氨酸、赖氨酸、色氨酸残基的试剂对酶活无明显影响,而作用于组氨酸、精氨酸和带羧基氨基酸残基的试剂使酶活降低。底物对化学修饰剂有保护作用。组氨酸、精氨酸和带羧基氨基酸(谷氨酸或天冬氨酸)残基为脱卤酶活力所必需。
Dehalogenase is an enzyme which catalyzes a-haloacid to a-hydroxyl acid. Chemical modification reactions of dehalogenase YL, 109 and H-2 were carried out by various reagents. The experimental results showed that the activity was not significantly altered by seryl lysyl and trpyl reagent but decreased by hisyl, arginyl and carboxyl reagent. Substitute could protect the active centre to chemical modification. It was indicated that hisyl, arginyl and carboxyl (glu or asp) residue would be essential for the acti vity of dehalogenase.
出处
《生物工程学报》
CAS
CSCD
北大核心
1996年第3期318-321,共4页
Chinese Journal of Biotechnology
关键词
脱卤酶
化学修饰
Dehalogenase, chemical modification
