ArticlePeerJ2017
Purification and biochemical characterization of recombinant
Article in PeerJ, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Effects of drought duration on terpene profiles, physiological responses, and terpene-related gene expression in rosemary.BMC plant biology · 2026Article
- Molecular insights into Valencene synthase (SgTPS-V) and its role in sesquiterpenoid biosynthesis.BMC plant biology · 2026Article
- Antimicrobial and cytotoxic activities of natural (Z)-13-docosenamide derived fromFrontiers in cellular and infection microbiology · 2025Article
- Cloning, Expression and Functional Characterization of a Novel α-Humulene Synthase, Responsible for the Formation of Sesquiterpene in Agarwood Originating fromCurrent issues in molecular biology · 2023Article
- Kinetic studies and homology modeling of a dual-substrate linalool/nerolidol synthase from Plectranthus amboinicus.Scientific reports · 2021Article
- Evolution of Terpene Synthases in Orchidaceae.International journal of molecular sciences · 2021Review
- Enhanced production of taxadiene in Saccharomyces cerevisiae.Microbial cell factories · 2020Article
- Functional Characterisation of New Sesquiterpene Synthase from the Malaysian Herbal Plant,Molecules (Basel, Switzerland) · 2018Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSesquiterpenes are 15-carbon terpenes synthesized by sesquiterpene synthases using farnesyl diphosphate (FPP) as a substrate. Recently, a sesquiterpene synthase gene that encodes a 65 kDa protein was isolated from the aromatic plant
methodsThe enzyme was purified in two steps using affinity and size exclusion chromatography. Enzyme assays were performed using the malachite green assay and enzymatic product was identified using gas chromatography-mass spectrometry (GC-MS) analysis. Sequence analysis of PmSTS was performed using multiple sequence alignment (MSA) against plant sesquiterpene synthase sequences. The homology model of PmSTS was generated using I-TASSER server.
resultsOur findings suggest that the recombinant PmSTS is mainly expressed as inclusion bodies and soluble aggregate in the DISCUSSION: The study has revealed that homogenous PmSTS protein can be obtained with the addition of glycerol in the protein buffer. The N-terminal truncation dramatically improved the homogeneity of PmSTS during protein purification, suggesting that the disordered N-terminal region may have caused the formation of soluble aggregate. We further show that the removal of the N-terminus disordered region of PmSTS does not affect the product specificity. The optimal temperature, optimal pH,
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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.