Probing the substrate binding modes and catalytic mechanisms of BLEG-1, a promiscuous B3 metallo-β-lactamase with glyoxalase II properties.

PLoS One · 2023 · PMC10482274 · PMID 37672512

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possibly significantno p-value reported

Enzyme activity of BLEG-1 variants determined the substrate binding modes in BLEG-1 Based on the MD analyses, five residues which are most possibly significant for both ampicillin and SLG binding in BLEG-1 are Ile-10, Phe-57, Arg-94, Leu-95, and Arg-159.

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