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V. G. Grigorenko, I. P. Andreeva, M. Yu. Rubtsova, V. V. Burmakin, I. V. Uporov, A. M. Egorov

Study of catalytic properties of recombinant β-lactamases TEM-1 and TEM-171 of molecular class A

Abstract

In this work preparation of recombinant β-lactamases TEM-1 and TEM-171 of molecular class A, characterized by a single amino acid substitutionof valineatposition84to isoleucine(Val84Ile), was studied. For the first time kinetic parameters for TEM-171 have been obtained with chromogenic substrate CENTA: KM eff= 23 µM, kcat= 102 s–1. Competitive type of β-lactamases inhibition by tazobactam was ascertained. The inhibition constants for tazobactam with CENTA as a substrate were as follows: 0.057 µM and 0.047 µM for recombinant β-lactamase TEM-1 and TEM-171, respectively. It was shown that Val84Ile substitution leads to a decrease of β-lactamase TEM-171 thermostability by 1.5 times.
Key words: recombinant β-lactamase TEM-1, TEM-171, CENTA, kinetic parameters, tazobactam, competitive type of inhibition.
Moscow University Chemistry Bulletin.
2015, Vol. 56, No. 6, P. 336
   

Copyright (C) Chemistry Dept., Moscow State University, 2002
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