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May 18, 2026Journal of the American Chemical Society0 citationsOpen Access

Dimerization-Dependent Trans-Domain Coupling Enables Intermediate Transfer in Fungal Haloacid Dehalogenase-Like Terpene Cyclases

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TCTzu‐Ho ChenKHKai-Fa HuangTCTing-Hung Chou

Key Points

  • This research aims to understand the mechanisms behind enzyme coupling in fungal terpene cyclases and their product selectivity.
  • Utilized structure-guided mutagenesis to define determinants of product selectivity.
  • Conducted assays with farnesyl mono- and thiopyrophosphate analogues.
  • Investigated phosphate-release kinetics to support cross-monomer coupling.
  • Identified key factors affecting product selectivity in dimeric AacA.
  • Observed distinct dephosphorylation capacities among enzyme variants.
  • Demonstrated the role of dimerization in enhancing intermediate transfer efficiency.

Abstract

-domain intermediate transfer. In addition, phosphate-release kinetics support cross-monomer TC-to-HAD coupling in dimeric AacA. Structure-guided mutagenesis and assays with farnesyl mono- and thiopyrophosphate analogues further define the determinants of product selectivity and the distinct dephosphorylation capacities of these enzymes. These findings expand fungal DTS enzymology and guide TC engineering.

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Cite This Study

Chen et al. (2026) studied this question.

synapsesocial.com/papers/6a0aac6d5ba8ef6d83b6fdedhttps://doi.org/10.1021/jacs.6c04151
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