Title

Authors

Affiliation

¹Biotechnology Unit, Directorate of Wheat Research Karnal, Haryana, India; ²Department of Biotechnology, Maharishi Markandeshwar University Mullana, Ambala, India; ³Crop Improvement Division, Directorate of Wheat Research Karnal, Haryana, India.

Email

neprads@gmail.com; *Corresponding author

Article Type

Hypothesis

Date

Received April 04, 2013; Revised April 11, 2013; Accepted April 22, 2013; Published June 29, 2013

ADP-glucose pyrophosphorylase (AGPase), a key enzyme involved in higher plant starch biosynthesis, is composed of pairs of large (LS) and small subunits (SS). Ample evidence has shown that the AGPase catalyzes the rate limiting step in starch biosynthesis in higher plants. In this study, we compiled detailed comparative information about ADP glucose pyrophosphorylase in selected plants by analyzing their structural features e.g. amino acid content, physico-chemical properties, secondary structural features and phylogenetic classification. Functional analysis of these proteins includes identification of important 10 to 20 amino acids long motifs arise because specific residues and regions proved to be important for the biological function of a group of proteins, which are conserved in both structure and sequence during evolution. Phylogenetic analysis depicts two main clusters. Cluster I encompasses large subunits (LS) while cluster II contains small subunits (SS).

Keywords

Molecular Docking, HCV NS3/4A protease, inhibitors, Binding interactions.

Citation

Rani et al.  Bioinformation 9(11): 572-576 (2013)

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.