Partial Purification and structure prediction of salinity induced NADP–dependent Sorbitol–6–phosphate dehydrogenase from ground nut

Alok Jha; Prof. Ramasare Prasad

Volume : IV, Issue : XI, November - 2015

Partial Purification and structure prediction of salinity induced NADP–dependent Sorbitol–6–phosphate dehydrogenase from ground nut

Alok Jha, Prof. Ramasare Prasad

Abstract :

 To study the role of sorbitol–6–phosphate dehydrogenase in sorbitol synthesis in leaves of groundnut, properties of the enzyme were investigated. The activity of the enzyme, which catalyzes an NADP–dependent oxidation of the substrate to glucose–6–phosphate, was detected. The enzyme was purified about 88 fold from leaves of ground nut (salinity induced) using gel filtration and ion exchange chromatography with DEAE–cellulose and Blue Sepharose. The enzyme showed its maximum activity within a oad pH range between 7 and 9 for glucose– 6– phosphate reduction. The structure was predicted based on target–template similarity and alignments, which showed a monomer structure. The enzyme has an aldo–keto reductase motif and a parallel 8 beta/8 alpha barrel motif and establishes a new motif for NADP binding oxidoreductases. The structure of the enzyme should allow for the rational design of inhibitors that might provide molecular understanding of the catalytic mechanism, as well as potential therapeutic agents.