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

Sanmugavelan, Ragaventhan and Teoh, Teow Chong and Roslan, Nurnadiah and Mohamed, Zulqarnain (2018) In vitro and in silico studies of chalcone synthase variant 2 in Boesenbergia rotunda and its substrate specificity. Turkish Journal of Biology, 42 (3). ISSN 1300-0152, DOI https://doi.org/10.3906/biy-1710-107.

Full text not available from this repository.
Official URL: https://doi.org/10.3906/biy-1710-107

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.

Item Type: Article
Funders: University of Malaya’s research grants RP032-15AFR and RP032C-15AFR
Uncontrolled Keywords: Cell suspension culture; Chalcone synthase; Homology modelling; Molecular docking
Subjects: Q Science > Q Science (General)
Q Science > QH Natural history
Divisions: Faculty of Science > Institute of Biological Sciences
Depositing User: Ms. Juhaida Abd Rahim
Date Deposited: 20 Mar 2019 04:24
Last Modified: 20 Mar 2019 04:25
URI: http://eprints.um.edu.my/id/eprint/20772

Actions (login required)

View Item View Item