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Literature DB >> 2694955

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

J Péduzzi¹, M Barthélémy, K Tiwari, D Mattioni, R Labia.

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.

Entities: Chemical Mutation

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Year: 1989 PMID： 2694955 PMCID： PMC172844 DOI： 10.1128/AAC.33.12.2160

Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN： 0066-4804 Impact factor: 5.191

25 in total

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22 in total

1. Automated thermal cycling is superior to traditional methods for nucleotide sequencing of bla(SHV) genes.

Authors: P A Bradford
Journal: Antimicrob Agents Chemother Date: 1999-12 Impact factor: 5.191

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Journal: Antimicrob Agents Chemother Date: 2000-10 Impact factor: 5.191

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Journal: Antimicrob Agents Chemother Date: 1990-11 Impact factor: 5.191

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