The Importance of the Negative Charge of Beta-lactam Compounds in the Interactions With Active-site Serine Dd-peptidases and Beta-lactamases

摘要: The interaction between various penicillins and cephalosporins the carboxylate group of which at C-3 or C-4 had been esterified amidated different penicillin-recognizing enzymes was studied. In general, our findings reinforced common assumption that an anionic position is necessary for effective acylation these enzymes. However, relative activities modified beta-lactams as inactivators Streptomyces R61 DD-peptidase substrates Bacillus licheniformis, albus G Enterobacter cloacae beta-lactamases did not fit a general scheme in intrinsic electronic geometric properties beta-lactam compounds would be sufficient to explain their substrate inactivator towards types investigated.