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This product has been discontinued
|Storage Temperature:||Below -10oC|
|Stability:||> 5 years under recommended storage conditions|
|Substrate For (Enzyme):||α-Galacturonidase|
|Assay Format:||Spectrophotometer, Microplate, Auto-analyser|
This product has been discontinued (read more).
High purity 4-Nitrophenyl-α-D-galacturonide for use in research, biochemical enzyme assays and in vitro diagnostic analysis. This is a colourimetric substrate for the measurement of α-galacturonidase (EC 184.108.40.206) activity.
Thompson, J., Pikis, A., Rich, J., Hall, B. G. & Withers, S. G. (2013). FEBS Letters, 587(6), 799-803.
The catalytic activity of the Family 4 glycosidase LplD protein, whose active site motif is CHEV, is unknown despite its crystal structure having been determined in 2008. Here we identify that activity as being an α-galacturonidase whose natural substrate is probably α-1, 4-di-galacturonate (GalUA2). Phylogenetic analysis shows that LplD belongs to a monophyletic clade of CHEV Family 4 enzymes, of which four other members are also shown to be galacturonidases. Family GH 4 enzymes catalyze the cleavage of the glycosidic bond, via a non-canonical redox-assisted mechanism that contrasts with Koshland’s double-displacement mechanism.Hide Abstract
Keegstra, K., English, P. D. & Albersheim, P. (1972). Phytochemistry, 11, 1873-1880.
The fungal plant pathogen, Collectotrichum lindemuthianum, was grown in culture with either galactose, arabinose or pectin as the carbon source resulting in the selective secretion of α-galactosidase, α-arabinofuranosidase and exopolygalacturonase, respectively. Each enzyme has been purified by ion exchange and gel permeation chromatography. In addition, a β-glucosidase was purified from the culture filtrate or arabinose grown fungus. The purified α-galactosidase and α-arabinosidase preparations were found to be essentially free of other carbohydrases while the β-glucosidase and exopolygalacturonase preparations contain contaminating activities.Hide Abstract
Marsh, C. A. & Levvy, G. A. (1958). Biochemical Journal, 68(4), 610-617.
In the first systematic study of the enzyme β-glucuronidase, Masamune showed that oxkidney preparations did not hydrolyse (-)-menthyl α-D-glucuronide, and this compound was also not hydrolysed by mouse-liver β-glucuronidase and by a snail preparation rich in β-glucuronidase and in other simple glycosidases. Nevertheless, although it is not so ubiquitous as the β-glucuronide residue, there is evidence for a naturally occurring α-conjugated glucuronic acid, for example in wheat straw. It has been inferred that uridine diphosphoglucuronic acid also has the α-configuration.Hide Abstract