The βD484N mutant of penicillin acylase from Escherichia coli is more resistant to inactivation by substrates and can effectively perform peptide synthesis in aqueous medium-Reference-Cited by-同舟云学术

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The βD484N mutant of penicillin acylase from Escherichia coli is more resistant to inactivation by substrates and can effectively perform peptide synthesis in aqueous medium

Published:2015-02 Issue: Volume:112 Page:66-68
ISSN:1381-1177
Container-title:Journal of Molecular Catalysis B: Enzymatic
language:en
Short-container-title:Journal of Molecular Catalysis B: Enzymatic

Author:

Shcherbakova Tatyana A.,Panin Nikolay V.,Suplatov Dmitry A.,Shapovalova Irina V.,Švedas Vytas K.

Funder

Russian Ministry for Science and Education

Russian Foundation for Basic Research

Publisher

Elsevier BV

Subject

Process Chemistry and Technology,Biochemistry,Bioengineering,Catalysis

Reference19 articles.

1. Industrial-scale manufacturing of pharmaceutical-grade bioactive peptides

2. Biomedical applications of dipeptides and tripeptides

3. Peptides as materials

4. Penicillin acylase-catalyzed peptide synthesis: a chemo-enzymatic route to stereoisomers of 3,6-diphenylpiperazine-2,5-dione

5. Penicillin acylase-catalyzed peptide synthesis in aqueous medium: a chemo-enzymatic route to stereoisomerically pure diketopiperazines

Cited by 1 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. Identification and characterization of an amidase from Leclercia adecarboxylata for efficient biosynthesis of L-phosphinothricin;Bioresource Technology;2019-10

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