Evidence map›Paper›PMID 39302551›Full record

ArticleMolecular biology reports2024

Isolation and characterisation of sesquiterpene synthase from aromatic orchid Phalaenopsis bellina (Rchb.f.) Christenson.

Ahmad Asnawi Mus, Jualang Azlan Gansau, Vijay Kumar, Nor Azizun Rusdi

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Article in Molecular biology reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 authors.

Ahmad Asnawi MusBioAgriTech Research Group (BioATR), Faculty of Science and Natural Resources, Universiti Malaysia Sabah, Jalan UMS, 88400, Kota Kinabalu, Sabah, Malaysia.
Jualang Azlan GansauBioAgriTech Research Group (BioATR), Faculty of Science and Natural Resources, Universiti Malaysia Sabah, Jalan UMS, 88400, Kota Kinabalu, Sabah, Malaysia.
Vijay KumarBiotechnology Research Institute, Universiti Malaysia Sabah, Jalan UMS, 88400, Kota Kinabalu, Sabah, Malaysia.
Nor Azizun RusdiTissue Culture Laboratory, Institute for Tropical Biology and Conservation, Universiti Malaysia Sabah, Jalan UMS, 88400, Kota Kinabalu, Sabah, Malaysia. azizun@ums.edu.my.

Funding

Ministry of Higher Education, Malaysia FRGS/1/2017/STG05/UMS/03/2Universiti Malaysia Sabah GUG0280-2/2018
6 · The paper itself

Abstract

backgroundPhalaenopsis bellina, an orchid native to Borneo, is renowned for its unique appearance. It releases distinct fragrances, which have been linked to the presence of terpenoids. However, the identification and study of sesquiterpene synthase in P. bellina remain limited. In this study, we examines the functional characterisation of terpene synthase (TPS) from P. bellina, known as PbTS, through recombinant protein expression and its manifestation in the flower. METHODS AND

resultsGene annotation of PbTS revealed that the inferred peptide sequence of PbTS comprises 1,680 bp nucleotides encoding 559 amino acids with an estimated molecular mass of 65.2 kDa and a pI value of 5.4. A similarity search against GenBank showed that PbTS shares similarities with the previously published partial sequence of P. bellina (ABW98504.1) and Phalaenopsis equestris (XP_020597359.1 and ABW98503.1). Intriguingly, the phylogenetic analysis places the PbTS gene within the TPS-a group. In silico analysis of PbTS demonstrated stable interactions with farnesyl pyrophosphate (FPP), geranyl pyrophosphate (GPP), and geranylgeranyl pyrophosphate (GGPP). To verify this activity, an in vitro enzyme assay was performed on the PbTS recombinant protein, which successfully converted FPP, GPP, and GGPP into acyclic sesquiterpene β-farnesene, yielding approximately 0.03 mg/L. Expressional analysis revealed that the PbTS transcript was highly expressed in P. bellina, but its level did not correlate with β-farnesene levels across various flowering time points and stages.

conclusionThe insights gained from this study will enhance the understanding of terpenoid production in P. bellina and aid in the discovery of novel fragrance-related genes in other orchid species.

Indexed as

Alkyl and Aryl TransferasesFlowersOrchidaceaePhylogenySesquiterpenesAmino Acid SequenceCloning, MolecularGene Expression Regulation, PlantPlant ProteinsPolyisoprenyl PhosphatesRecombinant ProteinsAlkyl and Aryl Transferasesfarnesyl pyrophosphatePlant ProteinsPolyisoprenyl PhosphatesRecombinant ProteinsSesquiterpenesterpene synthaseOrchidaceaePbTSPhalaenopsisß-farneseneterpene synthaseterpenoid

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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.