Biochemical characterization of the L1-like metallo-β-lactamase from Stenotrophomonas lactitubi

L1-like metallo-β-lactamases (MBLs) exhibit diversity and are highly conserved. Although the presence of the bla L1-like gene is known, the biochemical characteristics are unclear. This study aimed to characterize an L1-like MBL from Stenotrophomonas lactitubi . It showed 70.9–99.7% similarity to 50 L1-like amino acid sequences. The characteristic kinetic parameter was its high hydrolyzing efficiency for ampicillin and nitrocefin. Furthermore, L1-like from S. lactitubi was distinctly more susceptible to inhibition by EDTA than that to inhibition by 2,6-pyridinedicarboxylic acid.