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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Designed Water Capture in Terpene Synthase Catalysis.

Prabhakar L Srivastava1, David J Miller1, Rudolf K Allemann1

  • 1School of Chemistry, Cardiff University, Cardiff, UK.

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|March 12, 2026
PubMed
Summary
This summary is machine-generated.

Researchers engineered sesquiterpene synthases for specific product outcomes by altering key amino acids. This work provides a generalizable method for biocatalyst development, enabling the creation of novel sesquiterpenes for various applications.

Keywords:
enzyme engineeringprotein engineeringsolvationterpene synthase

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Area of Science:

  • Biochemistry
  • Enzymology
  • Organic Chemistry

Background:

  • Sesquiterpene synthases (SPS) produce diverse sesquiterpenes from farnesyl diphosphate through complex cyclization and rearrangement reactions.
  • The precise mechanisms governing the carbocationic intermediate's fate (deprotonation vs. water capture) remain incompletely understood.
  • Previous work engineered water capture in a specific SPS (SpSdS) via a G305E mutation.

Purpose of the Study:

  • To develop a generalized protocol for switching SPS function towards water capture.
  • To identify and characterize a novel selinadiene synthase (AsSdS) with potential for engineering.
  • To investigate the role of specific active site residues in controlling sesquiterpene product profiles.

Main Methods:

  • Bioinformatic analysis to identify novel sesquiterpene synthases.
  • Site-directed mutagenesis to create specific enzyme variants.
  • Enzymatic assays to characterize product formation and reaction mechanisms.

Main Results:

  • A novel selinadiene synthase (AsSdS) from Actinacidiphila soli was identified, naturally possessing glutamate at position 305 (E305).
  • Site-directed mutagenesis (G221T) in AsSdS successfully induced water capture, yielding selin-7(11)-en-4-ol.
  • Two key residue positions (G/E305 in Khelix and T/G221 in Hhelix) were identified as critical determinants of product outcome in selinadiene synthases.

Conclusions:

  • Subtle, predictable mutations in key active site residues (G/E305 and T/G221) reproducibly alter water capture and deprotonation pathways in selinadiene synthases.
  • This understanding of solvation effects can be leveraged to engineer other terpene synthases.
  • The study provides a foundation for developing biocatalysts with tailored product profiles for diverse applications.