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

Kageto Yamada¹, Yoshikazu Ishii¹, Kazuhiro Tateda¹

¹Department of Microbiology and Infectious Disease, Toho University School of Medicine, Tokyo, Japan.

Antimicrobial Agents and Chemotherapy

|February 8, 2024

Abstract:

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.

Keywords:

L1-like MBL Stenotrophomonas enzyme kinetics

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