ArticleNature chemistry2020
A monodomain class II terpene cyclase assembles complex isoprenoid scaffolds.
Article in Nature chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Enzymatic Prenylation of Proteins and Peptides: From Cysteine S-Prenylation to Tryptophan-Selective Biocatalysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Dimerization-Dependent Trans-Domain Coupling Enables Intermediate Transfer in Fungal Haloacid Dehalogenase-Like Terpene Cyclases.Journal of the American Chemical Society · 2026Article
- Unified genomic and chemical representations enable bidirectional biosynthetic gene cluster and natural product retrieval.Scientific reports · 2026Article
- BGC-MAC and BGC-MAP: Attention-Based Models for Biosynthetic Gene Cluster Classification and Product Matching.Journal of chemical information and modeling · 2026Article
- The Evolutionary History and Modern Diversity of Triterpenoid Cyclases.Molecular biology and evolution · 2025Article
- Structural insights into a bacterial terpene cyclase fused with haloacid Dehalogenase-like phosphatase.Chemical science · 2025Article
- Combining biocatalytic and radical retrosynthesis for efficient chemoenzymatic synthesis of natural products.Chemical Society reviews · 2025Review
- The evolutionary history and modern diversity of triterpenoid cyclases.bioRxiv : the preprint server for biology · 2025Article
- Synthesis of diverse terpenoid frameworks via enzyme-enabled abiotic scaffold hop.Nature chemistry · 2025Article
- Crystal structure and catalytic mechanism of drimenol synthase, an unusual bifunctional terpene cyclase-phosphatase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Engineering terpene synthases and their substrates for the biocatalytic production of terpene natural products and analogues.Chemical communications (Cambridge, England) · 2025Review
- Article
- Biocatalytic stereocontrolled head-to-tail cyclizations of unbiased terpenes as a tool in chemoenzymatic synthesis.Nature communications · 2024Article
- Class II terpene cyclases: structures, mechanisms, and engineering.Natural product reports · 2024Review
- Methods for the preparation and analysis of the diterpene cyclase fusicoccadiene synthase.Methods in enzymology · 2024Article
- Genome mining of labdane-related diterpenoids: Discovery of the two-enzyme pathway leading to (-)-sandaracopimaradiene in the fungusBeilstein journal of organic chemistry · 2024Article
- Vanadium haloperoxidases as noncanonical terpene synthases.Methods in enzymology · 2024Article
- Methods for the preparation and analysis of a bifunctional class II diterpene synthase, copalyl diphosphate synthase from Penicillium fellutanum.Methods in enzymology · 2024Article
- Identification, Heterologous Expression, and Characterization of the Tolypodiol Biosynthetic Gene Cluster through an Integrated Approach.ACS chemical biology · 2023Article
- Plant (di)terpenoid evolution: from pigments to hormones and beyond.Natural product reports · 2023Review
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7 authors.
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Abstract
Class II terpene cyclases, such as oxidosqualene and squalene-hopene cyclases, catalyse some of the most complex polycyclization reactions. They minimally exhibit a β,γ-didomain architecture that has been evolutionarily repurposed in a wide range of terpene-processing enzymes and likely resulted from a fusion of unidentified monodomain proteins. Although single domain class I terpene cyclases have already been identified, the corresponding class II counterparts have not been previously reported. Here we present high-resolution X-ray structures of a monodomain class II cyclase, merosterolic acid synthase (MstE). With a minimalistic β-domain architecture, this cyanobacterial enzyme is able to construct four rings in cytotoxic meroterpenoids with a sterol-like topology. The structures with bound substrate, product, and inhibitor provide detailed snapshots of a cyclization mechanism largely governed by residues located in a noncanonical enzyme region. Our results complement the few known class II cyclase crystal structures, while also indicating that archaic monodomain cyclases might have already catalyzed complex reaction cascades.
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