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Literature summary extracted from

  • Kester, H.C.M.; Benen, J.A.E.; Visser, J.
    The exopolygalacturonase from Aspergillus tubingensis is also active on xylogalacturonan (1999), Biotechnol. Appl. Biochem., 30, 53-57.
No PubMed abstract available

Application

EC Number Application Comment Organism
3.2.1.67 analysis studying fine structure of xylogalacturonan in pectin Aspergillus tubingensis
3.2.1.67 nutrition potent enzyme for production of D-galacturonate from pectin, starting compound in synthesis of ascorbic acid Aspergillus tubingensis
3.2.1.67 synthesis preparing methylated pectins Aspergillus tubingensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.67
-
 Aspergillus tubingensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.67 D-galactopyranuronic acid
-
 Aspergillus tubingensis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.67 Aspergillus tubingensis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.67 (1,4-alpha-D-galacturonide)n + H2O
-
 Aspergillus tubingensis D-galacturonate + digalacturonic acid + trigalacturonic acid
-
 ?
3.2.1.67 oligo-D-galacturonate + H2O
-
 Aspergillus tubingensis D-galacturonic acid
-
 ?
3.2.1.67 pectin + H2O apple pectin Aspergillus tubingensis digalacturonate + D-galacturonic acid
-
 ?
3.2.1.67 xylogalacturonan + H2O terminal galacturonic acid residue carries a single xylose substitution Aspergillus tubingensis xylogalacturonate
-
 ?