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<p>To further explore the catalytic versatility of <i>Penicillium expansum</i> lipase (PEL), we investigated and optimized its application in the Pudovik-Abramov reaction. Under environmentally friendly optimized conditions, PEL effectively catalyzed the reaction, yielding valuable α-hydroxyalkylphosphonates with efficiencies reaching up to 94%. Leveraging site-directed mutagenesis, we also probed the potential molecular basis underlying the enzymatic catalysis of the Pudovik-Abramov reaction. Our results demonstrate that although the catalytic mechanism for this reaction differs from that of the enzyme’s native hydrolysis activity, the catalytic histidine residue within the PEL catalytic triad retains an indispensable role in the Pudovik-Abramov reaction. This underscores that key structural elements of the lipase active site, such as the catalytic triad, constitute crucial molecular foundations for its catalytic promiscuity.</p> Graphical Abstract <p>PEL effectively catalyzed the Pudovik-Abramov reaction, yielding valuable α-hydroxyalkylphosphonates. The catalytic histidine residue within the PEL catalytic triadretains an indispensable role in the reaction.</p> <p></p>

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Catalytic Promiscuity of Penicillium expansum Lipase: Application in the Pudovik-Abramov Reaction and the Molecular Basis of its Catalysis

  • 期刊论文

  • 发表日期：

    2025年11月1日

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  • Yimei Zhou,
  • Min Su,
  • Mengjie Hu,
  • Lianghua Tang

摘要

To further explore the catalytic versatility of Penicillium expansum lipase (PEL), we investigated and optimized its application in the Pudovik-Abramov reaction. Under environmentally friendly optimized conditions, PEL effectively catalyzed the reaction, yielding valuable α-hydroxyalkylphosphonates with efficiencies reaching up to 94%. Leveraging site-directed mutagenesis, we also probed the potential molecular basis underlying the enzymatic catalysis of the Pudovik-Abramov reaction. Our results demonstrate that although the catalytic mechanism for this reaction differs from that of the enzyme’s native hydrolysis activity, the catalytic histidine residue within the PEL catalytic triad retains an indispensable role in the Pudovik-Abramov reaction. This underscores that key structural elements of the lipase active site, such as the catalytic triad, constitute crucial molecular foundations for its catalytic promiscuity.

Graphical Abstract

PEL effectively catalyzed the Pudovik-Abramov reaction, yielding valuable α-hydroxyalkylphosphonates. The catalytic histidine residue within the PEL catalytic triadretains an indispensable role in the reaction.