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Functional Characterization of Multidomain LPMOs from Marine Vibrio Species Reveals Modulation of Enzyme Activity by

Yong Zhou1,2,3, Eirik G Kommedal2, Zarah Forsberg2

  • 1School of Biomolecular Science and Engineering (BSE), Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong 21210, Thailand.

Biochemistry
|December 12, 2025
PubMed

Insights

Bacterial virulence factors called lytic polysaccharide monooxygenases (LPMOs) have their activity regulated by novel mechanisms. The GbpA3 domain in Vibrio cholerae GbpA prevents premature LPMO activation until chitin binding occurs.

Area of Science:

  • Microbiology
  • Enzymology
  • Structural Biology

Background:

  • Bacterial pathogens utilize multidomain enzymes, including lytic polysaccharide monooxygenases (LPMOs), for virulence.
  • The Vibrio cholerae virulence factor GbpA (VcGbpA) is a multidomain LPMO with N-terminal LPMO, GbpA2, GbpA3, and C-terminal chitin-binding (CBM73) domains.

Purpose of the Study:

  • To functionally characterize the multidomain LPMO VcGbpA and its homologue VhGbpA.
  • To elucidate the role of the GbpA2 and GbpA3 domains in LPMO activity and regulation.
  • To uncover the mechanism regulating LPMO activity in multidomain enzymes.

Main Methods:

  • In-depth functional characterization of full-length and truncated VcGbpA and VhGbpA variants.
  • Analysis of chitin binding and degradation properties.
  • Structural predictions and sequence conservation analyses.

Main Results:

  • The catalytic LPMO domains of VcGbpA and VhGbpA function similarly to single-domain LPMOs in chitin degradation.
  • The GbpA2 and GbpA3 domains influence chitin binding and degradation efficiency.
  • GbpA3 interacts with the LPMO catalytic copper site, preventing off-pathway reactions; CBM73 binding weakens this interaction, enabling substrate-activated LPMO function.

Conclusions:

  • GbpA3 acts as a regulatory domain, preventing premature LPMO activation.
  • Chitin binding by CBM73 is essential for activating LPMO activity.
  • This study reveals a novel mechanism for regulating multidomain LPMO activity.

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