ArticlePure and applied chemistry. Chimie pure et appliquee2010
Trinuclear Metal Clusters in Catalysis by Terpenoid Synthases.
Article in Pure and applied chemistry. Chimie pure et appliquee, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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Who cites it
89 citing papers in PubMed.
- Divergent Lineage of Terpene Synthases Establishes Terpenoid Biosynthesis in Brown Macroalgae.Journal of the American Chemical Society · 2026Article
- Reinvestigation of the mechanism and selectivity of 1,8-cineole synthase usingChemical science · 2026Article
- A methionine-lined active site governs carbocation stabilization and product specificity in a bacterial terpene synthase.FEBS letters · 2026Article
- Variations of terpenes profiling and functional characterization of terpene synthases in Agrimonia pilosa.BMC plant biology · 2026Article
- Structure and Mechanism of Avermitilol Synthase, a Sesquiterpene Cyclase That Generates a Highly Strained 6-6-3 Tricyclic Alcohol.Biochemistry · 2025Article
- Uncrossing the 'X': Characterization of alternative alleles for KSLX in Oryza.Phytochemistry · 2025Article
- Cryo-EM Structure of the Cyclase Domain and Evaluation of Substrate Channeling in a Bifunctional Class II Terpene Synthase.Biochemistry · 2025Article
- The initial dynamics of product release in terpene synthases-The case of CotB2.Protein science : a publication of the Protein Society · 2025Article
- Cryo-EM Structure of the Cyclase Domain and Evaluation of Substrate Channeling in a Bifunctional Class II Terpene Synthase.bioRxiv : the preprint server for biology · 2025Article
- Exploring evolutionary use of single residue switches for alternative product outcome in class II diterpene cyclases.Phytochemistry · 2025Article
- Structure of bifunctional variediene synthase yields unique insight on biosynthetic diterpene assembly and cyclization.Nature communications · 2025Article
- Single Point Mutation Abolishes Water Capture in Germacradien-4-ol Synthase.Chembiochem : a European journal of chemical biology · 2024Article
- Article
- Discovery of bifunctional diterpene cyclases/synthases in bacteria supports a bacterial origin for the plant terpene synthase gene family.Horticulture research · 2024Article
- Chemical and transcriptomic analyses of leaf trichomes from Cistus creticus subsp. creticus reveal the biosynthetic pathways of certain labdane-type diterpenoids and their acetylated forms.Journal of experimental botany · 2024Article
- Differential Substrate Sensing in Terpene Synthases from Plants and Microorganisms: Insight from Structural, Bioinformatic, and EnzyDock Analyses.Angewandte Chemie (International ed. in English) · 2024Article
- Unravelling the Function of the Sesquiterpene Cyclase STC3 in the Lifecycle ofInternational journal of molecular sciences · 2024Article
- Class II terpene cyclases: structures, mechanisms, and engineering.Natural product reports · 2024Review
- Structure of the prenyltransferase in bifunctional copalyl diphosphate synthase from Penicillium fellutanum reveals an open hexamer conformation.Journal of structural biology · 2024Article
- Methods for the preparation and analysis of the diterpene cyclase fusicoccadiene synthase.Methods in enzymology · 2024Article
29 more citing papers are in PubMed but not listed here.
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2 authors.
Funding
Abstract
Terpenoid synthases are ubiquitous enzymes that catalyze the formation of structurally and stereochemically diverse isoprenoid natural products. Many isoprenoid coupling enzymes and terpenoid cyclases from bacteria, fungi, protists, plants, and animals share the class I terpenoid synthase fold. Despite generally low amino acid sequence identity among these examples, class I terpenoid synthases contain conserved metal binding motifs that coordinate to a trinuclear metal cluster. This cluster not only serves to bind and orient the flexible isoprenoid substrate in the precatalytic Michaelis complex, but it also triggers the departure of the diphosphate leaving group to generate a carbocation that initiates catalysis. Additional conserved hydrogen bond donors assist the metal cluster in this function. Crystal structure analysis reveals that the constellation of three metal ions required for terpenoid synthase catalysis is generally identical among all class I terpenoid synthases of known structure.
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