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. 1989 Dec;33(12):2160–2163. 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 1, K Tiwari 1, D Mattioni 1, R Labia 1
PMCID: PMC172844  PMID: 2694955

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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Selected References

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