ROLE OF A BURIED ACID GROUP IN MECHANISM OF ACTION OF CHYMOTRYPSIN

被引：1099

作者：

BLOW, DM

BIRKTOFT, JJ

HARTLEY, BS

机构：

来源：

NATURE | 1969年 / 221卷 / 5178期

关键词：

D O I：

10.1038/221337a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The catalytic site of chymotrypsin contains an interior aspartic acid hydrogen-bonded to a histidine which in its turn is hydrogen-bonded to a serine. Polarization of the system due to the buried negative charge of the aspartic acid residue would make the serine oxygen strongly nucleophilic and would explain its reactivity towards amides and esters. © 1969 Nature Publishing Group.

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页码：337 / &

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