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Literature summary for 3.2.1.31 extracted from

  • Borisenkov, M.F.; Bakutova, L.A.; Latkin, D.S.; Golovchenko, V.V.; Vityazev, F.V.
    Interaction of microbial beta-glucuronidase with vegetable pectins (2011), J. Agric. Food Chem., 59, 9922-9926.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
pectin-protein complex adsorption of beta-glucuronidase on biopolymers is studied by the retention of the enzyme on the membrane of a concentrator with a pore diameter of 300 kDa and by native PAGE. Pectin-protein complexes (fractions PPC/CP and PPC/C) are established to increase the activity of beta-glucuronidase by 50 and 100%, respectively. There is a positive correlation between the increase of beta-glucuronidase activity in the presence of carbohydrates and enzyme adsorption on the polymers. The activity of the enzyme in the gel after electrophoresis of the PPC/+ beta-glucuronidase mixture is inversely proportional to the concentration of PPC/C in the mixture Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenolphthalein-beta-D-glucuronide + H2O
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Escherichia coli phenolphthalein + D-glucuronic acid
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?

Synonyms

Synonyms Comment Organism
beta-glucuronidase
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Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
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assay carried out at room temperature Escherichia coli