Comparative computational analysis of ADP Glucose Pyrophosphorylase in plants

Biotechnology Unit, Directorate Of Wheat Research Karnal, Haryana, India ,Saroj Rani,Ravish Chatrath,Anil Sharma,Pradeep Sharma

doi:10.6026/97320630009572

Biotechnology Unit, Directorate Of Wheat Research Karnal, Haryana, India , Saroj Rani + Show 3 more

Open Access

https://doi.org/10.6026/97320630009572

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Abstract

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).

Highlights

Starch is an important carbohydrate and the primary energy source in plants
The first enzyme in starch biosynthesis is the ADP-glucose pyrophosphorylase (AGPase) that catalyzes the conversion of Glc-1-P and ATP to ADP-glucose and pyrophosphate (PPi)
The results obtained in case of instability index and aliphatic index were contradictory while compared for AGPase analysis in rice, potato and Arabidopsis

Summary

Introduction

Starch is an important carbohydrate and the primary energy source in plants. It has numerous industrial applications as reviewed in Slattery et al [1, 6]. AGPase from higher plants has a heterotetrameric structure (ά2β2) composed of pairs of small (SS) and large (LS) subunits encoded by at least two different genes [5]. Maize (Zea mays) and rice (Oryza sativa), the two major cereals, show 93% identity in the amino acids sequence for the LS of AGPase enzyme.

Results

Conclusion