Tertiary structural similarity between a class A beta-lactamase and a penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase.
beta-Lactam antibiotics--the penicillins, cephalosporins and related compounds--act by inhibiting enzymes that catalyse the final stages of the synthesis of bacterial cell walls. Recent crystallographic studies of representative enzymes are beginning to reveal the structural bases of antibiotic specificity and mechanism of action, while intensive efforts are being made to understand the beta-lactamase enzymes that are largely responsible for bacterial resistance to these antibiotics. It has been suggested that the beta-lactamases and beta-lactam target enzymes may be evolutionarily related and some similarity of amino-acid sequence around a common active-site serine residue supports this idea. We present here the first evidence from a comparison of three-dimensional structures in support of this hypothesis: the structure of beta-lactamase I from Bacillus cereus is similar to that of the penicillin-sensitive D-alanyl-D-alanine carboxypeptidase-transpeptidase from Streptomyces R61.
D002268:Carboxypeptidases / Q000037:antagonists & inhibitors; D002267:Muramoylpentapeptide Carboxypeptidase / Q000037:antagonists & inhibitors; D010406:Penicillins / Q000494:pharmacology; D011487:Protein Conformation; D001618:beta-Lactamases
D010406:Penicillins; D002268:Carboxypeptidases; D002267:Muramoylpentapeptide Carboxypeptidase; D001618:beta-Lactamases