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A. M. Luhavaya, V. G. Grigorenko

Study of catalytic properties of recombinant class A TEM-1 b-lactamase and its iNhibition by sulbactam, tazobactam and clavulanic acid

Abstract

In this work was studied homogeneous preparation of recombinant class A TEM-1 b-lactamase; kinetic parameters obtained with chromogenic substrate CENTA are as follows: KM = 22 mM, V = 0,39 mM/s, kcat = 31,2 s-1, kcat/KM =1,4 mM-1s-1. Based on the comparison of determined Michaelis constant (KM = 22 mM) with literature data it is approved that recombinant enzyme is about 3 times more specific against CENTA than the native one (KM = 70 mM). It was ascertained competitive type of inhibition for sulbactam, tazobactam and clavulanic acid. For the first time the inhibition constants for recombinant b-lactamase TEM-1 with CENTA as a substrate for sulbactam, tazobactam, clavulanic acid (KI(sulbactam) = 0,43 mM, KI(tazobactam) = 0,041 mM, KI(clavulanic acid) = 0,046 mM) have been determined. It was shown that tazobactam and clavulanic acid are the most effective inhibitors for the recombinant b-lactamase as having the least value of KI and their inactivation influence can be accepted as identical.
Moscow University Chemistry Bulletin.
2010, Vol. 51, No. 3, P. 174
   

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