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Shaw Xian Au

As seen in: PLOS ONE
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Articles

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

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By Shaw Xian Au, Azyyati Mohd Padzil, Hiroyoshi Matsumura, Yahaya M Normi
| paperity.org
PLOS ONE, Sep 2023 BLEG-1 from Bacillus lehensis G1 is an evolutionary divergent B3 metallo-β-lactamase (MBL) that exhibited both β-lactamase and glyoxalase II (GLXII) activities. Sequence, phylogeny, biochemical and structural relatedness of BLEG-1 to B3 MBL and GLXII suggested BLEG-1 might be an intermediate in the evolutionary path of B3 MBL from GLXII.
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Probing the substrate binding modes and catalytic mechanisms of BLEG-1, a promiscuous B3 metallo-β-lactamase with glyoxalase II properties

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By Universiti Putra Malaysia, Shaw Xian Au, Azyyati Mohd Padzil, Malaysia Genome
| PLOS ONE
Loading metrics Open Access Peer-reviewed Research Article Citation: Au SX, Mohd Padzil A, Muhd Noor ND, Matsumura H, Raja Abdul Rahman RNZ, Normi YM (2023) Probing the substrate binding modes and catalytic mechanisms of BLEG-1, a promiscuous B3 metallo-β-lactamase with glyoxalase II properties. PLoS ONE 18(9): e0291012. https://doi.org/10.1371/journal.pone.0291012 Editor: Ahmed A.
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