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Penicillin Acylase: A Retrospective Study of the Kinetics and Thermodynamics of Practically Significant Reactions

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Abstract

This review considers the contribution of works carried out at the scientific school of Ilya Vasilievich Berezin to research on the kinetics and thermodynamics of penicillin acylase-catalyzed reactions. Methods for determining the activity of penicillin acylases, the reversibility of the enzymatic hydrolysis of a number of penicillins, cephalosporins, and related compounds, the influence of the β-lactam ring on the thermodynamics of the synthesis of new penicillins and cephalosporins by direct condensation as well as by acyl transfer, the issues of optimizing the conditions for enzymatic acyl transfer, and the use of supersaturated reagent solutions are discussed. The role of chromogenic substrates in the study of penicillin acylase, the possibility of using the methods of titration of active sites of the enzyme and the creation of “smart” biocatalysts based on penicillin acylase due to the formation of conjugates with stimulus-sensitive polymers are considered.

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Funding

This study was supported by the Russian Science Foundation, grant no. 21-71-30003.

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Correspondence to V. K. Švedas.

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Translated by M. Drozdova

Abbreviations and notation: 7-ADCA, 7-aminodeacetoxycephalosporanic acid; Phg, D-phenylglycine; CL, cephalexin; NIPAB, 2-nitro-5-(phenylacetyl)aminobenzoic acid; HPLC, high performance liquid chromatography.

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Panin, N.V., Guranda, D.T., Shapovalova, I.V. et al. Penicillin Acylase: A Retrospective Study of the Kinetics and Thermodynamics of Practically Significant Reactions. Moscow Univ. Chem. Bull. 78, 187–200 (2023). https://doi.org/10.3103/S0027131423040041

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