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Structural features related to hydrolytic activity against ceftazidime of plasmid-mediated SHV-type CAZ-5
J Péduzzi1, M Barthélémy, K Tiwari
1Muséum National d'Histoire Naturelle, Centre National de la Recherche Scientifique Unité de Recherche Associée, Paris, France.
Antimicrobial Agents and Chemotherapy
|December 1, 1989
Abstract:
Tryptic peptides of the novel ceftazidimase CAZ-5 were sequenced by manual Edman degradation and aligned according to strong homology (more than 98%) with SHV-1 and SHV-2 beta-lactamase sequences. CAZ-5 differed from SHV-1 by five amino acid substitutions. Unusually high activity of CAZ-5 towards ceftazidime was imputed to substitution of a Lys for a Glu at position 214 of the mature protein.