ArticleBioengineering (Basel, Switzerland)2022
Phylogenetic Analysis and Protein Modelling of Isoflavonoid Synthase Highlights Key Catalytic Sites towards Realising New Bioengineering Endeavours.
Article in Bioengineering (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Genome-Wide Identification and Characterization ofInternational journal of molecular sciences · 2025Article
- The Dose-Dependent Effect of Carbon Quantum Dots as a Photosynthesis Enhancer on Soybean Plant Growth.Nanomaterials (Basel, Switzerland) · 2025Article
- Systematic Engineering ofJournal of fungi (Basel, Switzerland) · 2024Article
- Protein Modelling Highlighted Key Catalytic Sites Involved in Position-Specific Glycosylation of Isoflavonoids.International journal of molecular sciences · 2023Article
- Bioprospecting microbes and enzymes for the production of pterocarpans and coumestans.Frontiers in bioengineering and biotechnology · 2023Review
- Combined analysis of inorganic elements and flavonoid metabolites reveals the relationship between flower quality and maturity ofFrontiers in plant science · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Isoflavonoid synthase (IFS) is a critical enzyme for the biosynthesis of over 2400 isoflavonoids. Isoflavonoids are an important class of plant secondary metabolites that have a range of pharmaceutical and nutraceutical properties. With growing interest in isoflavonoids from both research and industrial perspectives, efforts are being forwarded to enhance isoflavonoid production in-planta and ex-planta; therefore, in-silico analysis and characterisation of available IFS protein sequences are needed. The present study is the first-ever attempt toward phylogenetic analysis and protein modelling of available IFS protein sequences. Phylogenetic analysis has shown that IFS amino acid sequences have 86.4% pairwise identity and 26.5% identical sites, and the sequences were grouped into six different clades. The presence of a β-hairpin and extra loop at catalytic sites of
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Registered trials
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