Extreme Stabilization of a Thermolysin-like Protease by an Engineered Disulfide Bond-Reference-Cited by-同舟云学术

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Extreme Stabilization of a Thermolysin-like Protease by an Engineered Disulfide Bond

Published:1997-04 Issue:17 Volume:272 Page:11152-11156
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Mansfeld Johanna,Vriend Gert,Dijkstra Bauke W.,Veltman O. Rob,Van den Burg Bertus,Venema Gerard,Ulbrich-Hofmann Renate,Eijsink Vincent G.H.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference55 articles.

1. The Primary Structure ofBacillus cereusNeutral Proteinase and Comparison with Thermolysin andBacillus subtilisNeutral Proteinase

2. Nucleotide sequence and promoter region for the neutral protease gene from Bacillus stearothermophilus

3. Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein

4. A highly thermostable neutral protease from Bacillus caldolyticus: cloning and expression of the gene in Bacillus subtilis and characterization of the gene product

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