| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7754668 | Journal of Inorganic Biochemistry | 2016 | 10 Pages |
Abstract
Metallo-β-lactamases from non-pathogenic microorganism display functional promiscuity. Docking studies indicate that both β-lactam-based antibiotics and N-acyl homoserine lactones bind to the metal ions in the active site, forming a catalytically competent Michaelis complex. Kinetic measurements demonstrate that the Co(II) derivative of the enzymes is the most efficient lactonase.265
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Manfredi Miraula, Gerhard Schenk, NataÅ¡a MitiÄ,