| Literature DB >> 31413883 |
N V Panin1, M V Nikulin1,2, E S Tiurin2, V V Drobot1,2, I A Morozova1,2, V K Švedas1.
Abstract
The possibility of using amides of halogen-substituted acetic acids as acyl donors in penicillin acylase-catalyzed reactions has been investigated, and the ability of this group of compounds to inactivate enzymes in the course of the catalytic conversion has been established. The strongest inactivating effect was demonstrated by iodoacetamide and bromoacetamide. However, the negative contribution of this side activity can be minimized by decreasing the temperature, when the rate of acyl donor conversion by penicillin acylases is still high enough, but the impact of enzyme inactivation becomes less significant. The catalytic activity of penicillin acylase from Alcaligenes faecalis in the conversion of 2-haloacetamides was significantly (5-8 times) higher than that of penicillin acylase from Escherichia coli.Entities:
Keywords: 2-haloacetamides; Penicillin acylases; inactivation during the reaction; substrate specificity
Year: 2019 PMID: 31413883 PMCID: PMC6643344 DOI: 10.32607/20758251-2019-11-2-77-81
Source DB: PubMed Journal: Acta Naturae ISSN: 2075-8251 Impact factor: 1.845