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Literature summary for 3.2.1.139 extracted from

  • McKee, L.S.; Sunner, H.; Anasontzis, G.E.; Toriz, G.; Gatenholm, P.; Bulone, V.; Vilaplana, F.; Olsson, L.
    A GH115 alpha-glucuronidase from Schizophyllum commune contributes to the synergistic enzymatic deconstruction of softwood glucuronoarabinoxylan (2016), Biotechnol. Biofuels, 9, 002.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.139

Application

Application Comment Organism
degradation an enzymatic cocktail consisting of Agu115 with xylanase (Xyn10C), an alpha-L-arabinofuranosidase (AbfA), and a beta-xylosidase (XynB) achieves almost complete conversion of glucuronoarabinoxylan to arabinofuranose, xylopyranose, and methyl glucuronate monosaccharides. Addition of isoform Agu115 to the enzymatic cocktail contributes specifically to 25% of the conversion Schizophyllum commune

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Schizophyllum commune

Organism

Organism UniProt Comment Textmining
Schizophyllum commune
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
spruce gluconoarabinoxylan + H2O
-
 Schizophyllum commune 4-O-methyl-D-glucuronic acid + ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Schizophyllum commune

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 stable up to Schizophyllum commune

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.8
-
-
 Schizophyllum commune

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 8
-
 Schizophyllum commune

General Information

General Information Comment Organism
physiological function the enzyme removes (4-O-methyl)-glucuronic acid ((Me)GlcA) residues from polymeric and oligomeric xylan. The enzyme is required for the complete deconstruction of spruce glucuronoarabinoxylan and acts synergistically with other xylan-degrading enzymes, specifically a xylanase (Xyn10C), an alpha-L-arabinofuranosidase (AbfA), and a beta-xylosidase (XynB). Each enzyme in this mixture showed varying degrees of potentiation by the other activities, likely due to increased physical access to their respective target monosaccharides. The exo-acting Agu115 and AbfA are unable to remove all of their respective target side chain decorations from gluconoarabinoxylan, but their specific activity is significantly boosted by the addition of the endo-Xyn10C xylanase Schizophyllum commune