Mutation of Residue βF71 of Escherichia coli Penicillin Acylase Results in Enhanced Enantioselectivity and Improved Catalytic Properties
Author:
Publisher
Acta Naturae Ltd
Subject
Molecular Biology,Molecular Medicine,Biochemistry,Biotechnology
Link
http://actanaturae.ru/2075-8251/article/viewFile/10786/pdf
Cited by 7 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. PENICILLIN ACYLASE: A RETROSPECTIVE OF STUDYING THE KINETICS AND THERMODYNAMICS OF PRACTICALLY SIGNIFICANT REACTIONS;Lomonosov chemistry journal;2023-11-04
2. Penicillin Acylase: A Retrospective Study of the Kinetics and Thermodynamics of Practically Significant Reactions;Moscow University Chemistry Bulletin;2023-08
3. Specificity of Penicillin Acylases in Deprotection of N-Benzyloxycarbonyl Derivatives of Amino Acids;Acta Naturae;2023-05-03
4. Selectivity and kinetic modeling of penicillin G acylase variants for the synthesis of cephalexin under a broad range of substrate concentrations;Biotechnology and Bioengineering;2022-09-06
5. Industrial and Therapeutic Enzymes;Current Developments in Biotechnology and Bioengineering;2017
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