ArticleAnalytical biochemistry2012
An enzyme-coupled continuous fluorescence assay for farnesyl diphosphate synthases.
Article in Analytical biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- High-Throughput Profiling of Prenylelongases Enables the Assembly of Modified Prenoids.ACS chemical biology · 2026Article
- Functional characterization of a farnesyl diphosphate synthase from Dendrobium nobile Lindl.AMB Express · 2022Article
- Enzymatic Construction of DARPin-Based Targeted Delivery Systems Using Protein Farnesyltransferase and a Capture and Release Strategy.International journal of molecular sciences · 2022Article
- Zoledronic Acid as a Novel Dual Blocker of KIR6.1/2-SUR2 Subunits of ATP-Sensitive KPharmaceutics · 2021Article
- FDPS promotes glioma growth and macrophage recruitment by regulating CCL20 via Wnt/β-catenin signalling pathway.Journal of cellular and molecular medicine · 2020Article
- Article
- Study on the Correlation between Gene Expression and Enzyme Activity of Seven Key Enzymes and Ginsenoside Content in Ginseng in Over Time in Ji'an, China.International journal of molecular sciences · 2017Article
- Simultaneous Site-Specific Dual Protein Labeling Using Protein Prenyltransferases.Bioconjugate chemistry · 2015Article
- Site-specific labeling of proteins and peptides with trans-cyclooctene containing handles capable of tetrazine ligation.Chemical biology & drug design · 2014Article
- Engineering protein farnesyltransferase for enzymatic protein labeling applications.Bioconjugate chemistry · 2014Article
- Chemoenzymatic site-specific reversible immobilization and labeling of proteins from crude cellular extract without prior purification using oxime and hydrazine ligation.Current protocols in chemical biology · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Farnesyl diphosphate synthase (FDPS) catalyzes the conversion of isopentenyl diphosphate and dimethylallyl diphosphate to farnesyl diphosphate, a crucial metabolic intermediate in the synthesis of cholesterol, ubiquinone, and prenylated proteins; consequently, much effort has gone into developing inhibitors that target FDPS. Currently most FDPS assays either use radiolabeled substrates and are discontinuous or monitor pyrophosphate release and not farnesyl diphosphate (FPP) creation. Here we report the development of a continuous coupled enzyme assay for FDPS activity that involves the subsequent incorporation of the FPP product of that reaction into a peptide via the action of protein farnesyltransferase (PFTase). By using a dansylated peptide whose fluorescence quantum yield increases upon farnesylation, the rate of FDPS-catalyzed FPP production can be measured. We show that this assay is more sensitive than existing coupled assays, that it can be used to conveniently monitor FDPS activity in a 96-well plate format, and that it can reproduce IC(50) values for several previously reported FDPS inhibitors. This new method offers a simple, safe, and continuous method to assay FDPS activity that should greatly facilitate the screening of inhibitors of this important target.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.