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Updated: May 31, 2026

Apoplast-Extraction Based Method to Improve the Purity of Plant Produced Recombinant Protein
Published on: July 5, 2024
[Functions of plant apyrases]
Magdalena Wujak1, Michał Komoszyński
1Instytut Biologii Ogólnej i Molekularnej, Zakład Biochemii Uniwersytetu Mikołaja Kopernika, ul. Gagarina 7, 87-100 Toruń.
Abstract:
This publication presents results of the recent studies on plant NTPDases (apyrases). The structure and major physicochemical properties of this enzymes are reviewed. The attention has been paid to metabolic functions of apyrases from Solanum tuberosum and Arabidopsis thaliana. Apyrases constitute a family of proteins hydrolyzing phosphoanhydride bonds of nucleoside tri- and di-phosphates. They share common features like a similar structure, broad nucleotide substrate specificity and divalent cation requirement for their catalytic activity. The presence of plant NTPDases was detected in various cellular compartments. They are soluble or membrane-bound proteins. In hydrolytic processes catalyzed by activity of apoplastic apyrases and other ectoenzymes, adenine, ribose and orthophosphate are produced. These compounds are transported to the cell. Apyrases have been speculated to be involved in the regulation of starch synthesis and signal transmission. Their activity is necessary for development and growth of tubers and roots. Enzymes from leguminous plants activate the symbiosis with root nodule bacteria. Considering the fact, that NTPDases change the nucleotide concentration in cells and tissues, most of described functions may be related to the regulation of the energy charge of cell.
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