Structural features related to hydrolytic activity against ceftazidime of plasmid-mediated SHV-type CAZ-5 beta-lactamase.
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.
Péduzzi
J
J
Muséum National d'Histoire Naturelle, Centre National de la Recherche Scientifique Unité de Recherche Associée, Paris, France.
Barthélémy
M
M
Tiwari
K
K
Mattioni
D
D
Labia
R
R
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*
D002442:Ceftazidime; C062759:beta-lactamase CAZ-5; C062760:beta-lactamase SHV-2; D001618:beta-Lactamases