Digalacturonic acid (DGA), derived in vivo from pectin catabolism, is used for the co-crystallization of enzymes such as proteinase K. It is used in galacturonic acid metabolism research as a substrate to identify, differentiate and characterized endo- and exopolygalacturonase(s) and gluconase(s). DGA is used to study the transport of oligogalacturonides by systems such as the TogMNAB ABC transporter.
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Proteinase K, a subtilisin-like fungal protease, was crystallized from a cocktail of small molecules containing digalacturonic acid (DGA). The crystal structure was determined to 1.32 A resolution and refined to an R factor of 0.158. The final model contained, beside
The bacterium Erwinia chrysanthemi, which causes soft rot disease on various plants, is able to use pectin as a carbon source for growth. Knowledge of the critical step in pectin catabolism which allows the entry of pectic oligomers into the
Journal of industrial microbiology & biotechnology, 39(7), 1023-1029 (2012-03-01)
In Saccharomyces cerevisiae, an endopolygalacturonase encoded by the PGL1 gene catalyzes the random hydrolysis of the α-1,4 glycosidic linkages in polygalacturonic acid. To study the regulation of the PGL1 gene, we constructed a reporter vector containing the lacZ gene under
D-galacturonic acid is the most abundant component of pectin, one of the major polysaccharide constituents of plant cell walls. Galacturonic acid potentially is an important carbon source for microorganisms living on (decaying) plant material. A catabolic pathway was proposed in
Journal of molecular biology, 368(5), 1215-1222 (2007-04-03)
Family 28 glycoside hydrolases (polygalacturonases) are found in organisms across the plant, fungal and bacterial kingdoms, where they are central to diverse biological functions such as fruit ripening, biomass recycling and plant pathogenesis. The structures of several polygalacturonases have been
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