Nucleotide sequence of the SHV-5 beta-lactamase gene of a Klebsiella pneumoniae plasmid
- 1 December 1990
- journal article
- research article
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 34 (12), 2439-2441
- https://doi.org/10.1128/aac.34.12.2439
Abstract
The nucleotide sequence of the SHV-5 beta-lactamase gene, subcloned from a plasmid of Klebsiella pneumoniae, was determined. The amino acid changes thought to be responsible for the extended substrate profile of SHV-5 are Gly----Ser234 and Glu----Lys235. SHV-5 is identical to SHV-4, except for Leu----Arg201, which accounts for the difference in apparent pI of the two enzymes.This publication has 18 references indexed in Scilit:
- Structural features related to hydrolytic activity against ceftazidime of plasmid-mediated SHV-type CAZ-5 beta-lactamaseAntimicrobial Agents and Chemotherapy, 1989
- Molecular characterization of the gene encoding SHV-3 beta-lactamase responsible for transferable cefotaxime resistance in clinical isolates of Klebsiella pneumoniaeAntimicrobial Agents and Chemotherapy, 1989
- Comparative study of five plasmid-mediated ceftazidimases isolated in Klebsiella pneumoniaeJournal of Antimicrobial Chemotherapy, 1989
- Extended-spectrum beta-lactamasesAntimicrobial Agents and Chemotherapy, 1989
- Oxacillin‐hydrolysing β‐lactamasesEuropean Journal of Biochemistry, 1989
- Interactions of New Plasmid-Mediated -Lactamases with Third-Generation CephalosporinsClinical Infectious Diseases, 1988
- Single amino acid substitution between SHV‐1 β‐lactamase and cefotaxime‐hydrolyzing SHV‐2 enzymeFEBS Letters, 1988
- Bacterial Resistance to β-Lactam Antibiotics: Crystal Structure of β-Lactamase from Staphylococcus aureus PC1 at 2.5 Å ResolutionScience, 1987
- Close evolutionary relationship between the chromosomally encoded β lactamase gene of Klebsiellapneumoniae and the TEM β‐lactamase gene mediated by R plasmidsFEBS Letters, 1986
- The structure of β-lactamasesPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1980