Interaction of the pBR 322-coded RTEM beta-lactamase with substrates. Evidence for specific conformational transitions.
The rate of inactivation of RTEM-1 beta-lactamase by Pronase is accelerated by class A ('resistant') penicillins. Other substrates (class S penicillin and cephalosporins) protect against the inactivation. Cefoxitin, a semi-synthetic cephamycin, induces a more extensive, hysteretic response. In its presence the enzyme is inactivated by trypsin as well as by Pronase.
D002440:Cefoxitin / Q000494:pharmacology; D002511:Cephalosporins / Q000494:pharmacology; D010406:Penicillins / Q000494:pharmacology; D010957:Plasmids; D011402:Pronase / Q000494:pharmacology; D011487:Protein Conformation; D001618:beta-Lactamases / Q000378:metabolism*
D002511:Cephalosporins; D010406:Penicillins; D002440:Cefoxitin; D011402:Pronase; D001618:beta-Lactamases; C034413:beta-lactamase TEM-1