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

Autor:	Nikolay V. Panin, Irina V. Shapovalova, Tatyana A. Shcherbakova, Vytas K. Švedas, Dmitry A. Suplatov
Rok vydání:	2015
Předmět:	Aqueous medium Chemistry Process Chemistry and Technology Mutant Wild type Substrate (chemistry) Bioengineering medicine.disease_cause Biochemistry Catalysis chemistry.chemical_compound Penicillin Acylase Peptide synthesis medicine Escherichia coli
Zdroj:	Journal of Molecular Catalysis B: Enzymatic. 112:66-68
ISSN:	1381-1177
Popis:	The computationally designed βD484N mutant of penicillin acylase from Escherichia coli was shown to be more stable at alkaline conditions, resistant to inactivation by high substrate concentrations and able to catalyze preparative peptide synthesis in aqueous medium more effectively. The ability of the βD484N mutant to operate in alkaline aqueous medium allowed to reach up to 80% yields of d -phenylglycine-derived peptide synthesis from equimolar substrate mixtures while with the wild type penicillin acylase conversion was below 17%.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::bd9ef744f98225818b7501428dab3d2d https://doi.org/10.1016/j.molcatb.2014.11.015 Zobrazit plný text záznamu Full Text from ScienceDirect