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Title

 

 

 

 

 

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

 

Authors

 

Pravej Alam1, Usha Kiran2, M. Mobeen Ahmad1, Kamaluddin3, Mather Ali Khan4, Shalu Jhanwar M. Z. Abdin1,3*

 

Affiliation

 

1Centre for Transgenic Plant Development, Department of Biotechnology, Faculty of Science, 2Faculty of Engineering and Interdisciplinary Sciences, Jamia Hamdard, New Delhi, India, 3Department of Plant Breeding and Genetics, Faculty of Agriculture, Regional Research Station, Wadura, Sher-e-Kashmir University of Agriculture and Technology (J&K), India; 4School of Information Technology, Jawaharlal Nehru, University, New Delhi, India

 

Email

 

mzabdin@rediffmail.com

 

Article Type

 

Hypothesis

Date

 

Received January 02, 2010; accepted February 19, 2010; published March 31, 2010

Abstract

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.

 

Keywords

Artemisia annua; artemisinin; ADS3963 gene; homology modeling; phylogenetic tree; docking

 

Abbreviations

ADS = Amorpha-4, 11-diene synthase; FPP = farnesyl pyrophosphate; ORF = open reading frame; PCR = polymerase chain reaction

 

Citation

 

Alam et al., Bioinformation 4(9): 421-429 (2010)

Edited by

 

P. Kangueane

 

ISSN

 

0973-2063

 

Publisher

 

Biomedical Informatics

License

 

 

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.