Sequences of Homologous β-Lactamases from Clinical Isolates of Serratia marcescens with Different Substrate Specificities | Zendy

Naoki Matsumura | Zendy; Shinzaburo Minami | Zendy; Susumu Mitsuhashi | Zendy

Open Access

Sequences of Homologous β-Lactamases from Clinical Isolates of Serratia marcescens with Different Substrate Specificities

Author(s) -

Naoki Matsumura,

Shinzaburo Minami,

Susumu Mitsuhashi

Publication year - 1998

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.42.1.176

Subject(s) - serratia marcescens , microbiology and biotechnology , enterobacteriaceae infections , serratia , enterobacteriaceae , biology , homologous chromosome , bacteria , escherichia coli , genetics , gene , pseudomonas

Genes for two group 1 beta-lactamases, SRT-1 and SST-1, were sequenced. These beta-lactamases were produced by clinical isolates of Serratia marcescens, isolates GN16694 and GN19450, respectively. The resulting enzymes were 96% identical. SRT-1 hydrolyzed oxyimino cephalosporins, but SST-1 hardly hydrolyzed them. At residue 213 in the third motif, which is conserved among group 1 beta-lactamases, SRT-1 and SST-1 had Lys and Glu, respectively. By site-directed mutagenesis, the substitution of Glu by Lys at residue 213 in SST-1 resulted in an enzyme that hydrolyzed oxyimino cephalosporins.

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