Abstract

In higher plants, two pathways are implicated in the synthesis of isoprenoids: the mevalonate pathway and methyl-d-erythritol 4-phosphate (MEP) pathway. In MEP pathway, 1-deoxy-d-xylulose-5-phosphate synthase (DXS) enzyme catalyzes the first committed step and it is recognized as a rate-limiting enzyme. In this study, a partial cDNA encoding DXS1 domain isolated from Aconitum balfourii Stapf. was cloned and characterized (AbDXS1). Analysis of DXS domain was performed and we found that AbDXS1 had extensive similarities to other DXS1 proteins. It comprised highly conserved DRAG and PSD domains. A comparative analysis of expression patterns for AbDXS1 using the already existing transcriptome profiles of model plants suggests its role in primary metabolism which needs to be validated further through functional genomics. These data would be helpful for exploring the functions of DXS and its isoforms in MEP pathway of Aconitum balfourii Stapf.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call