Mimosa Pudica Apyrase Requires Polysaccharide and Ca2+ for the Activity

Overview

Journal Mol Cell Biochem

Publisher Springer

Specialty Biochemistry

Date 1998 Oct 27

PMID 9788742

Citations 1

Authors

R Ghosh

P C Sen

S Biswas

Affiliations

Soon will be listed here.

Abstract

Mimosa pudica Linn leaves with pulvini contain unique isoforms (I and II) of Apyrase enzyme (EC 3.6.1.5). The activity of isoform I depends on divalent cation Mn2+. This isoform is associated noncovalently with the polysaccharide, containing mainly of galactose and arabinose sugars. The apparent molecular mass of these 2 isoforms are 36 and 34 Kd respectively. The association of the polysaccharide with the isoform I has been found to be Ca2+ dependent which is endogenously present in this isoform. Removal of Ca2+ and polysaccharide from the enzyme (isoform I) leads to an inactivation. The enzyme activity can be restored when both Ca2+ and endogenous polysaccharide fraction were added at an optimal molar ratio of Ca2+:protein of 7:1. The endogenous polysaccharide can be replaced by the standard arabinogalactan. No other sugar or polysaccharide except the arabinogalactan can restore the apyrase activity. Calcium mediates a conformational change in the protein which helps in association of polysaccharide as evidenced from fluorometric and far UV-CD studies to restore the enzymic activity. Neither any interaction of the polysaccharide with the protein is detected in absence of Ca2+ nor the enzyme activity could be recovered under such condition.

Citing Articles

Purification and biochemical characterization of a novel ecto-apyrase, MP67, from Mimosa pudica.

Okuhata R, Takishima T, Nishimura N, Ueda S, Tsuchiya T, Kanzawa N Plant Physiol. 2011; 157(1):464-75.

PMID: 21788364 PMC: 3165892. DOI: 10.1104/pp.111.180414.

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