Comparative interactions of withanolides and sterols with two members of sterol glycosyltransferases from Withania somnifera.

ABSTRACT:

Background

Sterol glycosyltransferases (SGTs) are ubiquitous but one of the most diverse group of enzymes of glycosyltransferases family. Members of this family modulate physical and chemical properties of secondary plant products important for various physiological processes. The role of SGTs has been demonstrated in the biosynthesis of pharmaceutically important molecules of medicinal plants like Withania somnifera.

Results

Analysis suggested conserved behaviour and high similarity in active sites of WsSGTs with other plant GTs. Substrate specificity of WsSGTs were analysed through docking performance of WsSGTs with different substrates (sterols and withanolides). Best docking results of WsSGTL1 in the form of stable enzyme-substrate complex having lowest binding energies

SUBMITTER: Pandey V 

PROVIDER: S-EPMC4407318 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature