Protein engineering of the high-alkaline serine protease PB92 from Bacillus alcalophilus: functional and structural consequences of mutation at the S4 substrate binding pocket-Reference-Cited by-同舟云学术

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Protein engineering of the high-alkaline serine protease PB92 from Bacillus alcalophilus: functional and structural consequences of mutation at the S4 substrate binding pocket

Published:1992 Issue:5 Volume:5 Page:413-420
ISSN:1741-0126
Container-title:"Protein Engineering, Design and Selection"
language:en
Short-container-title:Protein Eng Des Sel

Author:

Teplyakov A.V.,van der Laan J.M.,Lammers A.A.,Kelders H.,Kalk K.H.,Misset O.,Mulleners L.J.S.M.,Dijkstra B.W.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/5/5/413/4417723/5-5-413.pdf

Cited by 40 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. In Silico Study of Camptothecin-Based Pro-Drugs Binding to Human Carboxylesterase 2;Biomolecules;2024-01-27

2. Molecular dynamics studies of disulfide bonds for enhancing the stability of serine protease PB92;New Journal of Chemistry;2024

3. Rational enzyme design by reducing the number of hotspots and library size;Chemical Communications;2024

4. Improving the Thermostability of Serine Protease PB92 from Bacillus alcalophilus via Site-Directed Mutagenesis Based on Semi-Rational Design;Foods;2023-08-16

5. Biochemical characterization of a novel oxidatively stable, halotolerant, and high‐alkaline subtilisin from Alkalihalobacillus okhensis Kh10‐101 ^T ;FEBS Open Bio;2022-07-06

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