TAILIEUCHUNG - In vitro and in silico studies of chalcone synthase variant 2 in Boesenbergia rotunda and its substrate specificity

In this study, transformation of BrCHS var 2 into B. rotunda cell suspension culture, followed by chalcone synthase enzymatic assay and HPLC analysis was conducted to investigate whether the substrate specificity for BrCHS var 2 is either cinnamoyl-CoA or p-coumaroyl-CoA. | Turkish Journal of Biology Turk J Biol (2018) 42: 213-223 © TÜBİTAK doi: Research Article In vitro and in silico studies of chalcone synthase variant 2 in Boesenbergia rotunda and its substrate specificity Ragaventhan SANMUGAVELAN, Teow Chong TEOH*, Nurnadiah ROSLAN, Zulqarnain MOHAMED Institute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, Malaysia Received: Accepted/Published Online: Final Version: Abstract: In this study, transformation of BrCHS var 2 into B. rotunda cell suspension culture, followed by chalcone synthase enzymatic assay and HPLC analysis was conducted to investigate whether the substrate specificity for BrCHS var 2 is either cinnamoyl-CoA or p-coumaroyl-CoA. The HPLC profile showed an increase in the amount of pinocembrin chalcone when cinnamoyl-CoA and malonyl-CoA were added but not p-coumaroyl-CoA. Molecular docking was performed to explore the binding of cinnamoyl-CoA and p-coumaroyl-CoA to BrCHS var 2 receptor and the docking results showed that cinnamoyl-CoA formed numerous hydrogen bonds and more negative docked energy than p-coumaroyl-CoA. Cinnamoyl-CoA showed good interactions with Cys 164 to initiate the subsequent formation of pinocembrin chalcone, whereas the hydroxyl group of p-coumaroyl-CoA formed an unfavorable interaction with Gln 161 that caused steric hindrance to subsequent formation of naringenin chalcone. Docked conformation analysis results also showed that malonyl-CoA formed hydrogen bonding with Cys 164, His 303, and Asn 336 residues in BrCHS var 2. The results show that cinnamoyl-CoA is the preferred substrate for BrCHS var 2. Key words: Chalcone synthase, cell suspension culture, homology modelling, molecular docking 1. Introduction Ginger was used as a food, spice, and herbal remedy over 2000 years ago. It is a monocot plant from the family Zingiberaceae that can be found widely in .

• Sinh học
• Chalcone synthase
• Cell suspension culture
• Homology modelling
• Molecular docking
• P coumaroyl CoA
• BMC Plant Biology
• Gene duplication
• Gene expression
• Gene family
• Chalcone synthase gene
• Drought stress
• Functional analysis
• Polyethylene glycol
• RNA extraction
• BMC Genetics
• Flavonoid biosynthesis
• Functional specialization
• Phylogenetic analysis
• Including chalcone synthase
• Chalcone isomerase
• Flavanone 3 hydroxylase
• Anthocyanidin synthase
• Flower development
• Transcription factor
• Flavonol synthase
• MYB114 exhibited
• G hirsutum L
• Fiber color
• Anthocyanidin reductase
• Leucoanthocyanidin reductase
• Agrobacterium tumefaciens
• Artemisia carvifolia Buch
• antioxidant assays
• Phenylalanine ammonia lyase
• Rol gene
• BMC Genomics
• Aspergillus sydowii
• Natural plants
• Anthocyanin synthesis pathway