Academic Journals Database
Disseminating quality controlled scientific knowledge

Isolation, characterization and structural studies of amorpha – 4, 11-diene synthase (ADS3963) from Arte a L. misia annu

Author(s): Pravej Alam | Usha Kiran2 | M. Mobeen Ahmad | Kamaluddin3 | Mather Ali Khan4 | Shalu Jhanwar M. Z. Abdin

Journal: Bioinformation
ISSN 0973-2063

Volume: 4;
Issue: 9;
Start page: 421;
Date: 2010;
Original page

Keywords: Artemisia annua | artemisinin | ADS3963 gene | homology modeling | phylogenetic tree | docking

With the escalating prevalence of malaria in recent years, artemisinin demand has placed considerable stress on its production worldwide. At present, the relative low-yield of artemisinin (0.01-1.1 %) in the source plant (Artemisia annua L. plant) has imposed a serious limitation in commercializing the drug. Amorpha-4, 11-diene synthase (ADS) has been reported a key enzyme in enhancing the artemisinin level in Artemisia annua L. An understanding of the structural and functional correlations of Amorpha-4, 11-diene synthase (ADS) may therefore, help in the molecular up-regulation of the enzyme. In this context, an in silico approach was used to study the ADS3963 (3963 bp) gene cloned by us, from high artemisinin (0.7-0.9% dry wt basis) yielding strain of A. annua L. The full-length putative gene of ADS3963 was found to encode a protein consisting of 533 amino acid residues with conserved aspartate rich domain. The isoelectric point (pI) and molecular weight of the protein were 5.25 and 62.2 kDa, respectively. The phylogenetic analysis of ADS genes from various species revealed evolutionary conservation. Homology modeling method was used for prediction of the 3D structure of ADS3963 protein and Autodock 4.0 version was used to study the ligand binding. The predicted 3D model and docking studies may further be used in characterizing the protein in wet laboratory.
Affiliate Program      Why do you need a reservation system?