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Molecular characterization of the SHV-11 beta-lactamase of Shigella dysenteriae.

ABSTRACT: A beta-lactamase with an M(r) of 29,000 and a pI of 7.6 was partially purified from a clinical isolate of Shigella dysenteriae. The bla gene encoded the SHV-11 enzyme carrying the substitution Leu-->Gln at position 35 and was linked to a strong promoter. This variant, unlike the prototype SHV-1 enzyme, hydrolyzed oxacillin, cloxacillin, and oxyiminocephalosporins such as cefotaxime.

SUBMITTER: Ahamed J 

PROVIDER: S-EPMC89421 | biostudies-literature | 1999 Aug

REPOSITORIES: biostudies-literature

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Molecular characterization of the SHV-11 beta-lactamase of Shigella dysenteriae.

Ahamed J J   Kundu M M  

Antimicrobial agents and chemotherapy 19990801 8

A beta-lactamase with an M(r) of 29,000 and a pI of 7.6 was partially purified from a clinical isolate of Shigella dysenteriae. The bla gene encoded the SHV-11 enzyme carrying the substitution Leu-->Gln at position 35 and was linked to a strong promoter. This variant, unlike the prototype SHV-1 enzyme, hydrolyzed oxacillin, cloxacillin, and oxyiminocephalosporins such as cefotaxime. ...[more]

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