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. 1989 Dec;33(12):2160-3.
doi: 10.1128/AAC.33.12.2160.

Structural features related to hydrolytic activity against ceftazidime of plasmid-mediated SHV-type CAZ-5 beta-lactamase

J Péduzzi  1 , M Barthélémy, K Tiwari, D Mattioni, R Labia
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Structural features related to hydrolytic activity against ceftazidime of plasmid-mediated SHV-type CAZ-5 beta-lactamase

J Péduzzi et al. Antimicrob Agents Chemother. 1989 Dec.

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.

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References

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