INCREASING THE THERMOSTABILITY OF THE NEUTRAL PROTEINASE OF BACILLUS-STEAROTHERMOPHILUS BY IMPROVEMENT OF INTERNAL HYDROGEN-BONDING

被引：17

作者：

EIJSINK, VGH ^{[1
]}

VRIEND, G ^{[1
]}

VANDERZEE, JR ^{[1
]}

VANDENBURG, B ^{[1
]}

VENEMA, G ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB,BIOCOMP PROGRAM,W-6900 HEIDELBERG,GERMANY

来源：

BIOCHEMICAL JOURNAL | 1992年 / 285卷

关键词：

D O I：

10.1042/bj2850625

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：

In an attempt to increase the thermostability of the neutral proteinase of Bacillus stearothermophilus the buried Ala-170 was replaced by serine. Molecular-dynamics simulations showed that Ser-170 stabilizes the enzyme by formation of an internal hydrogen bond. In addition, the hydroxy group of Ser-170 could contribute to stability by filling an internal cavity. After the introduction of the mutation, using site-directed-mutagenesis techniques, an increase in stability of 0.7 +/- 0.1-degrees-C was obtained.

引用

页码：625 / 628

页数：4

共 31 条

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