| Autor: |
Hammond, Gail G., Huber, Joann L., Greenlee, Mark L., Laub, Joanne B., Young, Katherine, Silver, Lynn L., Balkovec, James M., Pryor, KellyAnn D., Wu, Joseph K., Leiting, Barbara, Pompliano, David L., Toney, Jeffrey H. |
| Zdroj: |
FEMS Microbiology Letters; October 1999, Vol. 179 Issue: 2 p289-296, 8p |
| Abstrakt: |
IMP‐1 metallo‐β‐lactamase is a transferable carbapenem‐hydrolyzing enzyme found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescensand Klebsiella pneumoniae. Bacteria that express IMP‐1 show significantly reduced sensitivity to carbapenems and other β‐lactam antibiotics. A series of thioester derivatives has been shown to competitively inhibit purified IMP‐1. As substrates for IMP‐1, the thioesters yielded thiol hydrolysis products which themselves were reversible competitive inhibitors. The thioesters also increased sensitivity to the carbapenem L‐742,728 in an IMP‐1‐producing laboratory stain of Escherichia coli, but will need further modification to improve their activity in less permeable organisms such as Pseudomonasand Serratia. Nonetheless, the thioester IMP‐1 inhibitors offer an encouraging start to overcoming metallo‐β‐lactamase‐mediated resistance in bacteria. |
| Databáze: |
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