title: Structural features related to hydrolytic activity against ceftazidime of plasmid-mediated SHV-type CAZ-5 beta-lactamase.
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.
authors.affiliation: Muséum National d'Histoire Naturelle, Centre National de la Recherche Scientifique Unité de Recherche Associée, Paris, France.
authors.forename: J
authors.initials: J
authors.lastname: Péduzzi
authors.forename: M
authors.initials: M
authors.lastname: Barthélémy
authors.forename: K
authors.initials: K
authors.lastname: Tiwari
authors.forename: D
authors.initials: D
authors.lastname: Mattioni
authors.forename: R
authors.initials: R
authors.lastname: Labia
mesh_terms: D000595:Amino Acid Sequence; D002442:Ceftazidime / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006868:Hydrolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D010957:Plasmids; D001618:beta-Lactamases / Q000235:genetics / Q000378:metabolism*
chemical_list: D002442:Ceftazidime; C062759:beta-lactamase CAZ-5; C062760:beta-lactamase SHV-2; D001618:beta-Lactamases