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<p>Processive catalysis is a fundamental molecular mechanism to build and dismantle complex biopolymers such as nucleic acids, proteins and carbohydrates, underpinning a myriad of biotechnological applications. Here, we uncover a processive mechanism for the breakdown of β(1,3)-glucans, a widespread carbohydrate class. This mechanism involves a dynamic active site, which adopts a tunnel-like conformation upon substrate binding. For product release, the disruption of a salt bridge triggers an open conformation that interacts with the remnant substrate, essential for subsequent catalytic cycles. Molecular simulations reveal that this processive cleavage involves a non-canonical sugar conformation, a characteristic hitherto limited to exo-acting enzymes. Together, these findings establish the mechanistic basis for β(1,3)-glucan processive catalysis, from substrate recognition to tunnel formation, nucleophilic attack, intermediate state stabilization, product release and translocation. Ultimately, this work broadens the knowledge of β(1,3)-glucan breakdown, demonstrating that enzymatic processive catalysis is a conserved evolutionary strategy across all major classes of β-glucans.</p>

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Conformational gating mechanism for processive catalysis of β(1,3)-glucans

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年3月27日

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  • Gustavo H. B. Gimenis,
  • João P. M. Spadeto,
  • Felippe M. Colombari,
  • Renan Y. Miyamoto,
  • Paula M. R. Higasi,
  • Clelton A. Santos,
  • Fernanda Mandelli,
  • Marcele P. Martins,
  • Evandro A. Araújo,
  • Mariane N. Domingues,
  • Felipe J. Fuzita,
  • Amilton M. Oliveira,
  • Matheus C. Gazolla,
  • Camila R. Santos,
  • Gabriela F. Persinoti,
  • Harry Brumer,
  • Carme Rovira,
  • Carlos H. I. Ramos,
  • Mariana A. B. Morais,
  • Mario T. Murakami

摘要

Processive catalysis is a fundamental molecular mechanism to build and dismantle complex biopolymers such as nucleic acids, proteins and carbohydrates, underpinning a myriad of biotechnological applications. Here, we uncover a processive mechanism for the breakdown of β(1,3)-glucans, a widespread carbohydrate class. This mechanism involves a dynamic active site, which adopts a tunnel-like conformation upon substrate binding. For product release, the disruption of a salt bridge triggers an open conformation that interacts with the remnant substrate, essential for subsequent catalytic cycles. Molecular simulations reveal that this processive cleavage involves a non-canonical sugar conformation, a characteristic hitherto limited to exo-acting enzymes. Together, these findings establish the mechanistic basis for β(1,3)-glucan processive catalysis, from substrate recognition to tunnel formation, nucleophilic attack, intermediate state stabilization, product release and translocation. Ultimately, this work broadens the knowledge of β(1,3)-glucan breakdown, demonstrating that enzymatic processive catalysis is a conserved evolutionary strategy across all major classes of β-glucans.