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Antimicrobial Agents and Chemotherapy, January 1998, p. 176-179, Vol. 42, No. 1
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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

Naoki Matsumura,1,* Shinzaburo Minami,2 and Susumu Mitsuhashi1

Episome Institute, 2220 Kogure, Fujimi-mura, Seta-gun Gunma,1 and Research Laboratories, Toyama Chemical Co., Ltd., 2-4-1 Shimo-okui, Toyama-city, Toyama, 930,2 Japan

Received 12 March 1997/Returned for modification 22 July 1997/Accepted 22 October 1997

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.

* Corresponding author. Mailing address: Research Laboratories, Toyama Chemical Co., Ltd., 2-4-1 Shimo-okui, Toyama-city, Toyama, 930 Japan. Phone: 81-764-31-8268. Fax: 81-764-31-8208.

Antimicrobial Agents and Chemotherapy, January 1998, p. 176-179, Vol. 42, No. 1
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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