Cross-linking preserves conformational changes induced in penicillinase by its substrates.
Exopenicillinase of Bacillus cereus 569/H was cross-linked with toluene 2,4-diisocyanate in the presence of cephalothin, cloxacillin or no substrate. The derivatives show significant differences in susceptibility to inactivation by heat, urea, iodination or proteolysis. Such differences can be predicted from the contrasting effects of these substrates on the conformation of the enzyme.
D002512:Cephalothin / Q000494:pharmacology; D003023:Cloxacillin / Q000494:pharmacology; D003432:Cross-Linking Reagents; D003485:Cyanates; D004355:Drug Stability; D006358:Hot Temperature; D010068:Oxacillin / Q000494:pharmacology; D010405:Penicillinase; D011487:Protein Conformation / Q000187:drug effects; D014051:Toluene 2,4-Diisocyanate; D014508:Urea; D001618:beta-Lactamases
D003432:Cross-Linking Reagents; D003485:Cyanates; D014051:Toluene 2,4-Diisocyanate; D014508:Urea; D010405:Penicillinase; D001618:beta-Lactamases; D003023:Cloxacillin; D002512:Cephalothin; D010068:Oxacillin