Improving the diastereoselectivity of penicillin G acylase for ampicillin synthesis from racemic substrates
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,Bioengineering,Biotechnology
Link
http://academic.oup.com/peds/article-pdf/25/3/135/4323499/gzr065.pdf
Reference20 articles.
1. Drug delivery approaches to overcome bacterial resistance to β-lactam antibiotics
2. The Use of Chromogenic Reference Substrates for the Kinetic Analysis of Penicillin Acylases
3. The role of hydrophobic active-site residues in substrate specificity and acyl transfer activity of penicillin acylase
4. Characterization of the β-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies
5. Structural and kinetic studies on ligand binding in wild-type and active-site mutants of penicillin acylase
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3. Design and synthesis of thermosensitive target segment resin with precisely controlled distance between immobilization sites for immobilization of penicillin G acylase;Pigment & Resin Technology;2023-01-27
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