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PMID:9449282
| Citation |
Matsumura, N, Minami, S and Mitsuhashi, S (1998) Sequences of homologous beta-lactamases from clinical isolates of Serratia marcescens with different substrate specificities. Antimicrob. Agents Chemother. 42:176-9 |
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| Abstract |
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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| Keywords |
Amino Acid Sequence; Cephalosporins/metabolism; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Alignment; Sequence Homology, Amino Acid; Serratia marcescens/enzymology; Serratia marcescens/genetics; Substrate Specificity; beta-Lactamases/genetics; beta-Lactamases/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0008800: beta-lactamase activity |
ECO:0000315: |
F |
Table 2 |
complete | ||||
|
enables |
GO:0008800: beta-lactamase activity |
ECO:0000315: mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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