Rhamnogalacturonan I galactosyltransferase: Detection of enzyme activity and its hyperactivation.

08:00 EDT 4th July 2019 | BioPortfolio

Summary of "Rhamnogalacturonan I galactosyltransferase: Detection of enzyme activity and its hyperactivation."

Rhamnogalacturonan I (RG-I), one of the pectic components of the plant cell wall, is composed of a backbone of repeating disaccharide units of rhamnose and galacturonic acid, and side chains, such as galactans, arabinans, and arabinogalactans. The activity of RG-I galactosyltransferase, which transfers galactosyl residues to rhamnosyl residues in the RG-I backbone, has not been detected until now. Here, we detected galactosyltransferase activity in azuki bean epicotyls using fluorogenic RG-I oligosaccharide acceptors. This enzyme prefers oligosaccharides with a degree of polymerization more than 9. The enzyme activity was detected in the Golgi apparatus, which is the site of pectin synthesis. In vitro hyperactivation of this enzyme was also observed. Moreover, enzyme activity was increased up to 40-fold in the presence of cationic surfactants or polyelectrolytes.


Journal Details

This article was published in the following journal.

Name: Plant physiology and biochemistry : PPB
ISSN: 1873-2690
Pages: 173-178


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