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Literature summary extracted from

  • Takayanagi, T.
    Enzymological studies on isomalto-dextranase from Arthrobacter globiformis (2002), J. Appl. Glycosci., 49, 57-62.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.94 expressed in Escherichia coli Arthrobacter globiformis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.94 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide specifically modifies carboxyl residues Arthrobacter globiformis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.94 69000
-
 SDS-PAGE Arthrobacter globiformis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.94 Arthrobacter globiformis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.94
-
 Arthrobacter globiformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.94 dextran + H2O enzyme hydrolyzes alpha-1,6-glucosidic linkages of dextran or isomalto-oligosaccharides to release exolytically alpha-isomaltose from the non-reducing ends Arthrobacter globiformis alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc
-
 ?
3.2.1.94 pullulan + H2O enzyme also has a weak isopullulanase activity Arthrobacter globiformis isopanose
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.94 65
-
-
 Arthrobacter globiformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.94 5.3
-
-
 Arthrobacter globiformis