Abstract
The subclass B2 metallo-β-lactamase (MBL) Sfh-I from Serratia fonticola UTAD54 was cloned and over-expressed in Escherichia coli. The recombinant protein binds one equivalent of zinc, as shown by mass spectrometry, and preferentially hydrolyzes carbapenem substrates. However, compared to other B2 MBLs, Sfh-I also shows limited hydrolytic activity against some additional substrates and is not inhibited by a second equivalent of zinc. These data confirm Sfh-I to be a subclass B2 metallo-β-lactamase with some distinctive properties.
Translated title of the contribution | Biochemical characterization of Sfh-I, the subclass B2 metallo-{beta}-lactamase from Serratia fonticola UTAD54 |
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Original language | English |
Pages (from-to) | 5392 - 5395 |
Number of pages | 4 |
Journal | Antimicrobial Agents and Chemotherapy |
Volume | 55 |
DOIs | |
Publication status | Published - Nov 2011 |