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

Enzyme Activation Galactosyltransferases / analysis Hydrogen-Ion Concentration Oligosaccharides / metabolism Pectins / metabolism Plant Proteins / analysis Substrate Specificity Vigna / enzymology
Galactosyltransferase Hyperactivation Pectin Plant cell wall Rhamnogalacturonan I

Journal

Plant physiology and biochemistry : PPB
ISSN: 1873-2690
Titre abrégé: Plant Physiol Biochem
Pays: France
ID NLM: 9882449

Informations de publication

Date de publication:
Sep 2019
Historique:
received: 09 06 2019
revised: 03 07 2019
accepted: 03 07 2019
pubmed: 13 7 2019
medline: 18 12 2019
entrez: 13 7 2019
Statut: ppublish

Résumé

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.

Identifiants

DOI: 10.1016/j.plaphy.2019.07.008 PMID: 31299599
pubmed: 31299599
pii: S0981-9428(19)30287-6
doi: 10.1016/j.plaphy.2019.07.008
pii:
doi:

Substances chimiques

Oligosaccharides 0
Plant Proteins 0
rhamnogalacturonan I 0
Pectins 89NA02M4RX
Galactosyltransferases EC 2.4.1.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

173-178

Informations de copyright

Copyright © 2019 Elsevier Masson SAS. All rights reserved.

Auteurs

Naoki Matsumoto (N)

College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan.

Yuto Takenaka (Y)

Ritsumeikan Global Innovation Research Organization, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan.

Bussarin Wachananawat (B)

College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan.

Hiroyuki Kajiura (H)

College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan.

Tomoya Imai (T)

Research Institute for Sustainable Humanosphere, Kyoto University, Uji, Kyoto, 611-0011, Japan.

Takeshi Ishimizu (T)

College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan; Ritsumeikan Global Innovation Research Organization, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan. Electronic address: ishimizu@fc.ritsumei.ac.jp.

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Classifications MeSH

questionsmedicales.fr › Métabolisme › Activation enzymatique › Rhamnogalacturonan I galactosyltransferase:...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › Glycosyltransferase › Hexosyltransferases › Galactosyltransferases › Rhamnogalacturonan I galactosyltransferase:...
questionsmedicales.fr › Phénomènes chimiques › Concentration en ions d'hydrogène › Rhamnogalacturonan I galactosyltransferase:...
questionsmedicales.fr › Glucides › Polyosides › Oligosaccharides › Rhamnogalacturonan I galactosyltransferase:...
questionsmedicales.fr › Mélanges complexes › Produits biologiques › Préparations à base de plantes › Pectine › Rhamnogalacturonan I galactosyltransferase:...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines végétales › Rhamnogalacturonan I galactosyltransferase:...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Spécificité du substrat › Rhamnogalacturonan I galactosyltransferase:...
questionsmedicales.fr › Eucaryotes › Viridiplantae › Streptophyta › Embryophyta › Tracheobionta › Magnoliopsida › Fabaceae › Vigna › Rhamnogalacturonan I galactosyltransferase:...