REEXAMINATION OF THE ROLE OF ASP20 IN CATALYSIS BY BACTERIOPHAGE-T4 LYSOZYME

被引：51

作者：

HARDY, LW ^{[1
]}

POTEETE, AR ^{[1
]}

机构：

[1] UNIV MASSACHUSETTS,DEPT MOLEC GENET & MICROBIOL,WORCESTER,MA 01655

来源：

BIOCHEMISTRY | 1991年 / 30卷 / 39期

关键词：

D O I：

10.1021/bi00103a010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Replacement of Asp20 in T4 lysozyme by Cys produces a variant with (1) nearly wild-type specific activity, (2) a newly acquired sensitivity to thiol-modifying reagents, and (3) a pH-activity profile that is very similar to that of the wild-type enzyme. These results indicate that the residue at position 20 has a significant nucleophilic function rather than merely an electrostatic role. The intermediate in catalysis by lysozyme is probably a covalent glycosyl-enzyme instead of the ion pair originally proposed.

引用

页码：9457 / 9463

页数：7

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