In Silico Analysis of Ent-Kaurene Synthase shows Similar Functional Domain with Levopimaparadiene Synthase Involved in Biosynthesis of Ginkgolide

Background Ginkgo biloba is popularly known as living fossil. This plant is very popular due to presence of its novel phyto-constituents like ginkgolide and bilobalide. Its posses very high amount of flavonoid and terpene trilactones and posses high antioxidant activity. Ginkgolide and bilobalide are diterpenes and popularly known as terpene trilactone. The biosynthetic pathways for synthesis of terpene trilactone is yet to elucidate, but little and debatable information is present so far. The major gene levopimaradiene synthase is considered as the precursor enzyme for synthesis of ginkgolide molecule. Materials and Methods: Chloroplast precursor ent-kaurene synthase gene was downloaded from SWISS-PROT database and OsEnt-Kaurene gene was downloaded from rice genome annotation project. Multiple sequence alignment using clustalW show, both of them share common domain structure and conserved amino acid motif with levopimaradiene synthase which involved in diterpene synthesis. Results and discussion: Molecular analysis shows, ent-kaurene synthase shows similar domain structure with levopimaradiene synthase and involved in synthesis of ent-kaurene. The molecular structure of ent-kaurene resembles with the basic structure of ginkgolide. So, levopimaradiene synthase may evolved as chloroplast ent-kaurene synthase in higher plants and involved in diterpene synthesis.