Engineering thermolysin-like proteases whose stability is largely independent of calcium

被引：17

作者：

Veltman, OR

Vriend, G

vandenBurg, B

Hardy, F

Venema, G

Eijsink, VGH

机构：

[1] UNIV GRONINGEN,DEPT GENET,INST BIOMOL SCI & BIOTECHNOL,NL-9751 NN HAREN,NETHERLANDS

[2] EUROPEAN MOL BIOL LAB,D-69117 HEIDELBERG,GERMANY

[3] NLVF,LAB MICROBIAL GENE TECHNOL,N-1432 AS,NORWAY

来源：

FEBS LETTERS | 1997年 / 405卷 / 02期

关键词：

calcium binding; thermal stability; thermolysin; autolysis; unfolding pathway;

D O I：

10.1016/S0014-5793(97)00193-2

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：

Thermal stability of the thermolysin-like protease produced by Bacillus stearothermophilus (TLP-ste) is highly dependent on calcium at concentrations in the millimolar range. We describe the rational design and production of a fully active TLP-ste variant whose stability is only slightly dependent on calcium concentration. (C) 1997 Federation of European Biochemical Societies.

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收藏

页码：241 / 244

页数：4

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