Baldin S M, Shcherbakova T A, Švedas V K
Lomonosov Moscow State University, Belozersky Institute of Physicochemical Biology, Leninskie gory 1, bldg. 40, 119991, Moscow, Russia.
Lomonosov Moscow State University, Faculty of Chemistry, Leninskie gory 1, bldg. 3, 119991, Moscow, Russia.
Acta Naturae. 2019 Jan-Mar;11(1):23-28.
,-transpeptidase 2 from plays a key role in the formation of nonclassical 3-3 peptidoglycan cross-links in a pathogen's cell wall making it resistant to a broad range of penicillin antibiotics. The conditions of cultivation, isolation, and purification of recombinant ,-transpeptidase 2 from have been optimized in this study. Oxidation of the free SH groups of catalytic cysteine Cys354 is an important factor causing the inactivation of the enzyme, which occurs during both the expression and storage of enzyme preparations. The biochemical characteristics of purified ,-transpeptidase 2 and ,-transpeptidase 2 lacking domain A were determined; the kinetic constants of enzyme-catalyzed nitrocefin transformation were evaluated.
