ReviewIUBMB life2021
Structure, catalysis, and inhibition mechanism of prenyltransferase.
Review in IUBMB life, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Farnesol and geranylgeraniol in plant reproduction: insights from Arabidopsis and beyond.Journal of experimental botany · 2026Review
- Genetic blueprint of herbaceous peony floral scent: evidence from terpene synthase, Nudix hydrolase, and prenyltransferase.Horticulture research · 2026Article
- Impaired cortical actin dynamics via lanosterol-dependent HMG-CoA reductase downregulation mediates IFN-α-induced mast cell stabilization.The Journal of biological chemistry · 2026Article
- Enzymatic Prenylation of Proteins and Peptides: From Cysteine S-Prenylation to Tryptophan-Selective Biocatalysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- A methionine-lined active site governs carbocation stabilization and product specificity in a bacterial terpene synthase.FEBS letters · 2026Article
- A FungalJournal of agricultural and food chemistry · 2026Article
- Characterization of an (E, E)-farnesyl pyrophosphate synthase in Saxifraga stolonifera involved in triterpenoid biosynthesis.Plant molecular biology · 2026Article
- Genome mining reveals the unique function of UbiA-type prenyltransferase in Laetiporus sulphureus.Natural products and bioprospecting · 2026Article
- Structural classification, biosynthesis, metabolic engineering and ecological functions for the terpenes produced in tobacco.Frontiers in plant science · 2026Review
- A somatic multiple myeloma mutation unravels a mechanism of oligomerization-mediated product inhibition in GGPPS.The FEBS journal · 2025Article
- Protein Prenylation Makeovers in Plants: Insights into Substrate Diversification.International journal of molecular sciences · 2025Review
- Recent Advances in the Synthesis and Biological Applications of Prenylated Chalcones.International journal of molecular sciences · 2025Review
- Structure-Activity Relationship of an All-α-helical Prenyltransferase Reveals the Mechanism of Indole Prenylation.Biochemistry · 2025Article
- Stable Isotopic Labeling of Dimethylallyl Pyrophosphate (DMAPP) Reveals Compartmentalization of Isoprenoid Biosynthesis during Sporulation inJournal of the American Chemical Society · 2025Article
- Structures of Mycobacterium tuberculosis isoprenyl diphosphate synthase Rv2173 in substrate-bound forms.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Structure-function insights into the dual role of African swine fever virus pB318L: A typical geranylgeranyl-diphosphate synthase and a nuclear import protein.Virologica Sinica · 2025Article
- Synthesis, Bioproduction and Bioactivity of Perillic Acid-A Review.Molecules (Basel, Switzerland) · 2025Review
- Recent Research Progress on the Chemical Constituents, Pharmacology, and Pharmacokinetics ofMolecules (Basel, Switzerland) · 2024Review
- Coatings Based on Essential Oils for Combating Antibiotic Resistance.Antibiotics (Basel, Switzerland) · 2024Review
- Unravelling the Function of the Sesquiterpene Cyclase STC3 in the Lifecycle ofInternational journal of molecular sciences · 2024Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Isoprenoids, also known as terpenes or terpenoids, represent a large family of natural products composed of five-carbon isopentenyl diphosphate or its isomer dimethylallyl diphosphate as the building blocks. Isoprenoids are structurally and functionally diverse and include dolichols, steroid hormones, carotenoids, retinoids, aromatic metabolites, the isoprenoid side-chain of ubiquinone, and isoprenoid attached signaling proteins. Productions of isoprenoids are catalyzed by a group of enzymes known as prenyltransferases, such as farnesyltransferases, geranylgeranyltransferases, terpenoid cyclase, squalene synthase, aromatic prenyltransferase, and cis- and trans-prenyltransferases. Because these enzymes are key in cellular processes and metabolic pathways, they are expected to be potential targets in new drug discovery. In this review, six distinct subsets of characterized prenyltransferases are structurally and mechanistically classified, including (1) head-to-tail prenyl synthase, (2) head-to-head prenyl synthase, (3) head-to-middle prenyl synthase, (4) terpenoid cyclase, (5) aromatic prenyltransferase, and (6) protein prenylation. Inhibitors of those enzymes for potential therapies against several diseases are discussed. Lastly, recent results on the structures of integral membrane enzyme, undecaprenyl pyrophosphate phosphatase, are also discussed.
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