IMPROVING THE THERMOSTABILITY OF THE NEUTRAL PROTEASE OF BACILLUS-STEAROTHERMOPHILUS BY REPLACING A BURIED ASPARAGINE BY LEUCINE

被引：31

作者：

EIJSINK, VGH

VANDERZEE, JR

VANDENBURG, B

VRIEND, G

VENEMA, G

机构：

[1] CTR BIOL SCI,DEPT MOLEC GENET,KERKLAAN 30,9751 NN HAREN,NETHERLANDS

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

来源：

FEBS LETTERS | 1991年 / 282卷 / 01期

关键词：

THERMOSTABILITY; NEUTRAL PROTEASE; BURIED ASPARAGINE; BACILLUS-STEAROTHERMOPHILUS;

D O I：

10.1016/0014-5793(91)80434-5

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：

Amino acids buried in the hydrophobic interior of a protein with polar side chain atoms, which are not involved in hydrogen bonding or electrostatic interactions, have an adverse effect on protein stability. Replacing such residues by hydrophobic ones may render a protein more stable. Asparagine 241, which is buried in the neutral protease of Bacillus stearothermophilus, was replaced by leucine by site-directed mutagenesis. This mutation increased the stability of the protein by 0.7 +/- 0.1 degree.

引用

页码：13 / 16

页数：4

共 23 条

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