Sequences of Homologous β-Lactamases from Clinical Isolates of Serratia marcescens with Different Substrate Specificities
| Autor: | Susumu Mitsuhashi, Naoki Matsumura, Shinzaburo Minami |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
endocrine system
Molecular Sequence Data Sequence alignment medicine.disease_cause beta-Lactamases Substrate Specificity Microbiology Mechanisms of Resistance medicine Humans Pharmacology (medical) Amino Acid Sequence Site-directed mutagenesis Escherichia coli Peptide sequence Serratia marcescens Antibacterial agent Pharmacology chemistry.chemical_classification Sequence Homology Amino Acid biology biology.organism_classification Enterobacteriaceae Cephalosporins Infectious Diseases Enzyme Biochemistry chemistry Mutagenesis Site-Directed human activities Sequence Alignment |
| Zdroj: | Antimicrobial Agents and Chemotherapy. 42:176-179 |
| ISSN: | 1098-6596 0066-4804 |
| DOI: | 10.1128/aac.42.1.176 |
| Popis: | Genes for two group 1 β-lactamases, SRT-1 and SST-1, were sequenced. These β-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 β-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. |
| Databáze: | OpenAIRE |
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