Changes in proton-magnetic-resonance spectra during aminolysis and enzymic hydrolysis of cephalosporins.
1. Changes in proton-magnetic-resonance spectra were followed during the reaction of cephalosporins, deacetylcephalosporins, deacetoxycephalosporins and a Delta(2)-cephalosporin with ND(3) in D(2)O. 2. Changes in proton-magnetic-resonance spectra were also followed during the hydrolysis of a cephalosporin and a deacetylcephalosporin in D(2)O with a beta-lactamase. 3. Structures for the reaction products are proposed. 4. The signals obtained after aminolysis of the beta-lactam ring of a cephalosporin indicate that the reaction is accompanied by expulsion of the acetoxy group as acetate, formation of a double bond in the Delta(4)-position and the appearance of an exocyclic methylene group. 5. Aminolysis of deacetyl- and deacetoxycephalosporins can occur without immediate structural changes in the dihydrothiazine ring. 6. In contrast, the ring structure of the first product of enzymic hydrolysis of a deacetylcephalosporin is apparently identical with that of the product of aminolysis of the cephalosporin itself.
D000641:Ammonia; D002511:Cephalosporins; D055598:Chemical Phenomena; D002621:Chemistry; D003903:Deuterium; D009682:Magnetic Resonance Spectroscopy; D010400:Penicillin G; D010405:Penicillinase; D013057:Spectrum Analysis; D014466:Ultraviolet Rays
D002511:Cephalosporins; D000641:Ammonia; D003903:Deuterium; D010405:Penicillinase; D010400:Penicillin G