ArticleInternational journal of molecular sciences2012
Enzymatic properties and mutational studies of chalcone synthase from Physcomitrella patens.
Article in International journal of molecular sciences, 2012. 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, 20 citations in OpenAlex.
- Integrative structural and physicochemical characterization of chalcone synthase enzymes from medicinal plants using AlphaFold, molecular docking, and molecular dynamics.Scientific reports · 2026Article
- Article
- New Insights on Cyclization Specificity of Fungal Type III Polyketide Synthase, PKSIIIIndian journal of microbiology · 2018Article
- FoldX as Protein Engineering Tool: Better Than Random Based Approaches?Computational and structural biotechnology journal · 2018Review
- Genetically modified proteins: functional improvement and chimeragenesis.Bioengineered · 2015Review
- Molecular and Biochemical Analysis of Chalcone Synthase from Freesia hybrid in flavonoid biosynthetic pathway.PloS one · 2015Article
- Targeting death receptor TRAIL-R2 by chalcones for TRAIL-induced apoptosis in cancer cells.International journal of molecular sciences · 2012Article
- Effect of β-cyclodextrin complexation on solubility and enzymatic conversion of naringin.International journal of molecular sciences · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PpCHS is a member of the type III polyketide synthase family and catalyses the synthesis of the flavonoid precursor naringenin chalcone from p-coumaroyl-CoA. Recent research reports the production of pyrone derivatives using either hexanoyl-CoA or butyryl-CoA as starter molecule. The Cys-His-Asn catalytic triad found in other plant chalcone synthase predicted polypeptides is conserved in PpCHS. Site directed mutagenesis involving these amino acids residing in the active-site cavity revealed that the cavity volume of the active-site plays a significant role in the selection of starter molecules as well as product formation. Substitutions of Cys 170 with Arg and Ser amino acids decreased the ability of the PpCHS to utilize hexanoyl-CoA as a starter molecule, which directly effected the production of pyrone derivatives (products). These substitutions are believed to have a restricted number of elongations of the growing polypeptide chain due to the smaller cavity volume of the mutant's active site.
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