Evidence map›Paper›PMID 42018231›Full record

ArticleBiotechnology letters2026

Molecular, structural and functional characterization of flavonol synthase gene and its encoded protein in Millettia pinnata.

Garima Kumari, Hemanti Kumari, Vinod Kumar Nigam, Dev Mani Pandey

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Article in Biotechnology letters, 2026. 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 · The record

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5 · Who and what money

Authors and funding

4 authors.

Garima KumariDepartment of Bioengineering and Biotechnology, Birla Institute of Technology, Mesra, Ranchi, 835215, Jharkhand, India.
Hemanti KumariDepartment of Bioengineering and Biotechnology, Birla Institute of Technology, Mesra, Ranchi, 835215, Jharkhand, India.
Vinod Kumar NigamDepartment of Bioengineering and Biotechnology, Birla Institute of Technology, Mesra, Ranchi, 835215, Jharkhand, India.
Dev Mani PandeyDepartment of Bioengineering and Biotechnology, Birla Institute of Technology, Mesra, Ranchi, 835215, Jharkhand, India. dmpandey@bitmesra.ac.in.ORCID http://orcid.org/0000-0002-0711-9966

Funding

Department of Science and Technology, Ministry of Science and Technology, India IF180386
6 · The paper itself

Abstract

Millettia pinnata (M. pinnata) is a medicinally important plant containing many phytoconstituents capable of curing various diseases. Flavonol synthase (FLS, EC 1.14.20.6) has a significant role in flavonoid biosynthesis like kaempferol having various pharmacological properties. The present study aimed to characterize the FLS gene and its encoded protein (MpFLS) in M. pinnata comprehensively. FLS gene was characterized by isolating RNA from M. pinnata leaves, cDNA synthesis, PCR-based amplification of the desired FLS gene, sequencing of the PCR amplified product and sequence analysis followed by detailed protein-protein interaction and protein flexibility analysis. PCR product sequencing and analysis revealed that the full-length cDNA of M. pinnata FLS contains a 952-base pair long open reading frame (ORF) encoding 234 amino acids that has been submitted to NCBI (OM469017). The NCBI blastp analysis of 234 amino acid sequences of FLS shows 81.9% similarity to Vigna unguilata, whereas blastn analysis exhibited 83.31% identity to Clitoria ternatea L. that belongs to the 2OG-FeII Oxy superfamily. In silico characterization of primary, secondary, and tertiary structure, docking of MpFLS with dihydrokaempferol showed a strong binding (-10.0 kcal mol⁻

Indexed as

MillettiaOxidoreductasesPlant ProteinsAmino Acid SequenceModels, MolecularMolecular Docking Simulationflavonol synthaseOxidoreductasesPlant ProteinsFlavonol synthaseIn silico characterizationMillettia pinnataPolymerase chain reactionSequencing

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