ReviewMethods in enzymology2024
Mechanistic docking in terpene synthases using EnzyDock.
Review in Methods in enzymology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Chemoenzymatic Synthesis of (4R,7R)-Zingiberene Enables Construction of nor-Sesquiterpene Semiochemical Analogs.Chembiochem : a European journal of chemical biology · 2026Article
- A methionine-lined active site governs carbocation stabilization and product specificity in a bacterial terpene synthase.FEBS letters · 2026Article
- Template-Based Docking Using Automated Maximum Common Substructure Identification with EnzyDock: Mechanistic and Inhibitor Docking.Journal of chemical information and modeling · 2025Article
- CHARMM-GUIJournal of chemical theory and computation · 2025Article
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Authors and funding
3 authors.
Funding
Abstract
Terpene Synthases (TPS) catalyze the formation of multicyclic, complex terpenes and terpenoids from linear substrates. Molecular docking is an important research tool that can further our understanding of TPS multistep mechanisms and guide enzyme design. Standard docking programs are not well suited to tackle the unique challenges of TPS, like the many chemical steps which form multiple stereo-centers, the weak dispersion interactions between the isoprenoid chain and the hydrophobic region of the active site, description of carbocation intermediates, and finding mechanistically meaningful sets of docked poses. To address these and other unique challenges, we developed the multistate, multiscale docking program EnzyDock and used it to study many TPS and other enzymes. In this review we discuss the unique challenges of TPS, the special features of EnzyDock developed to address these challenges and demonstrate its successful use in ongoing research on the bacterial TPS CotB2.
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