ArticlePloS one2014
A high-throughput colorimetric screening assay for terpene synthase activity based on substrate consumption.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 63 citations in OpenAlex.
- Engineered microorganisms unlock a new era of diterpenoid biomanufacturing: recent advances and future perspectives.Bioresources and bioprocessing · 2026Review
- Rapid analysis of terpenes produced by fermentation using flow injection analysis coupled to APCI MS.Analytical methods : advancing methods and applications · 2026Article
- Engineering terpene synthases and their substrates for the biocatalytic production of terpene natural products and analogues.Chemical communications (Cambridge, England) · 2025Review
- Biosynthesis Progress of High-Energy-Density Liquid Fuels Derived from Terpenes.Microorganisms · 2024Review
- Product Profiles of Promiscuous Enzymes Can be Altered by Controlling In Vivo Spatial Organization.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Decoding Catalysis by Terpene Synthases.ACS catalysis · 2023Review
- Functional mining of novel terpene synthases from metagenomes.Biotechnology for biofuels and bioproducts · 2022Article
- Predictive Engineering of Class I Terpene Synthases Using Experimental and Computational Approaches.Chembiochem : a European journal of chemical biology · 2022Review
- Validation of an insertion-engineered isoprene synthase as a strategy to functionalize terpene synthases.RSC advances · 2021Article
- Protein engineering strategies for microbial production of isoprenoids.Metabolic engineering communications · 2020Review
- Synthetic biology, combinatorial biosynthesis, and chemo‑enzymatic synthesis of isoprenoids.Journal of industrial microbiology & biotechnology · 2020Review
- Emerging molecular biology tools and strategies for engineering natural product biosynthesis.Metabolic engineering communications · 2020Review
- Recent Development of Extremophilic Bacteria and Their Application in Biorefinery.Frontiers in bioengineering and biotechnology · 2020Review
- An automated pipeline for the screening of diverse monoterpene synthase libraries.Scientific reports · 2019Article
- The isoprenoid alcohol pathway, a synthetic route for isoprenoid biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Genetically engineered biosynthetic pathways for nonnatural CScientific reports · 2019Article
- Construction of a pathway to C50-ε-carotene.PloS one · 2019Article
- High-Throughput Screening of a 2-Keto-L-Gulonic Acid-ProducingFrontiers in bioengineering and biotechnology · 2019Article
- Development of Transcription Factor-Based Designer Macrolide Biosensors for Metabolic Engineering and Synthetic Biology.ACS synthetic biology · 2018Article
- Estimating the success of enzyme bioprospecting through metagenomics: current status and future trends.Microbial biotechnology · 2016Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Terpene synthases catalyze the formation of a variety of terpene chemical structures. Systematic mutagenesis studies have been effective in providing insights into the characteristic and complex mechanisms of C-C bond formations and in exploring the enzymatic potential for inventing new chemical structures. In addition, there is growing demand to increase terpene synthase activity in heterologous hosts, given the maturation of metabolic engineering and host breeding for terpenoid synthesis. We have developed a simple screening method for the cellular activities of terpene synthases by scoring their substrate consumption based on the color loss of the cell harboring carotenoid pathways. We demonstrate that this method can be used to detect activities of various terpene synthase or prenyltransferase genes in a high-throughput manner, irrespective of the product type, enabling the mutation analysis and directed evolution of terpene synthases. We also report the possibility for substrate-specific screening system of terpene synthases by taking advantage of the substrate-size specificity of C30 and C40 carotenoid pathways.
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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.