Tanya A. Murphy
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Tanya A. Murphy has a total of 4 co-authors. Here are the top co-authors by number of shared publications:
Alan M. Simm
Department of Pathology and Microbiology, University of Bristol, Bristol BS8 1TD, United Kingdom
1 shared publication- Mark Alexander Toleman
Department of Infection and Immunity, Cardiff University, Cardiff, UK
1 shared publication Ronald N. Jones
The Jones Group/JMI Laboratories, North Liberty, Iowa
1 shared publication- Timothy Rutland Walsh
Ineos Oxford Institute for Antimicrobial Research, Department of Biology, University of Oxford, Oxford OX1 3RE, UK
1 shared publication
Latest Publications
- Open Access
- 1 February 2003
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 47 (2) , 582-587
Biochemical Characterization of the Acquired Metallo-β-Lactamase SPM-1 fromPseudomonas aeruginosa
SPM-1 is a new metallo-β-lactamase recently identified inPseudomonas aeruginosastrain 48-1997A, isolated in Sao Paulo, Brazil. Kinetic analysis demonstrated that SPM-1 has a broad hydrolytic profile across a wide range of β-lactam antibiotics. Considerable variation was observed within the penicillin, cephalosporin, and carbapenem subfamilies; however, on the whole, SPM-1 appears to preferentially hydrolyze cephalosporins. The highestkcat/Kmratios (in micromolar per second) overall were observed for this subgroup. The hydrolytic profile of SPM-1 bears the most similarity to that of the metallo-β-lactamase IMP-1, yet for the most part, SPM-1 haskcat/Kmvalues higher than those of IMP-1. Zinc chelator studies established that progressive inhibition of SPM-1 by EDTA, dipicolinic acid, and 1-10-o-phenanthroline demonstrated a biexponential pattern in which none of the chelators completely inhibited SPM-1. A homology model of SPM-1 was developed on the basis of the IMP-1 crystal structure, which showed the protein folding and active-site structure characteristic of metallo-β-lactamases and which provides an explanation for the kinetic profiles observed.
- 1 February 2003
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 47 (2) , 582-587
Open AccessBiochemical Characterization of the Acquired Metallo-β-Lactamase SPM-1 fromPseudomonas aeruginosa
SPM-1 is a new metallo-β-lactamase recently identified inPseudomonas aeruginosastrain 48-1997A, isolated in Sao Paulo, Brazil. Kinetic analysis demonstrated that SPM-1 has a broad hydrolytic profile across a wide range of β-lactam antibiotics. Considerable variation was observed within the penicillin, cephalosporin, and carbapenem subfamilies; however, on the whole, SPM-1 appears to preferentially hydrolyze cephalosporins. The highestkcat/Kmratios (in micromolar per second) overall were observed for this subgroup. The hydrolytic profile of SPM-1 bears the most similarity to that of the metallo-β-lactamase IMP-1, yet for the most part, SPM-1 haskcat/Kmvalues higher than those of IMP-1. Zinc chelator studies established that progressive inhibition of SPM-1 by EDTA, dipicolinic acid, and 1-10-o-phenanthroline demonstrated a biexponential pattern in which none of the chelators completely inhibited SPM-1. A homology model of SPM-1 was developed on the basis of the IMP-1 crystal structure, which showed the protein folding and active-site structure characteristic of metallo-β-lactamases and which provides an explanation for the kinetic profiles observed.