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

L1-like metallo-beta-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.