Biochemical Characterization of Sfh-I, a Subclass B2 Metallo-β-Lactamase from Serratia fonticola UTAD54

• Published in: Antimicrobial Agents and Chemotherapy Vol. 55; no. 11; pp. 5392 - 5395
• Main Authors: Fonseca, Fátima, Arthur, Christopher J, Bromley, Elizabeth H. C, Samyn, Bart, Moerman, Pablo, Saavedra, Maria José, Correia, António, Spencer, James
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for Microbiology 01.11.2011
• Subjects: Antibiotics. Antiinfectious agents. Antiparasitic agents; beta-lactamase; beta-Lactamases; beta-Lactamases - genetics; beta-Lactamases - metabolism; Biological and medical sciences; Carbapenems - metabolism; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; mass spectrometry; Mechanisms of Resistance; Medical sciences; Pharmacology. Drug treatments; recombinant proteins; Serratia; Serratia - enzymology; Serratia fonticola; zinc; Characterization; Bacteria; Biochemistry; Serratia; Enterobacteriaceae
• ISSN: 0066-4804; 1098-6596
• DOI: 10.1128/AAC.00429-11

The subclass B2 metallo-β-lactamase (MBL) Sfh-I from Serratia fonticola UTAD54 was cloned and overexpressed 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.