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Literature summary extracted from

  • Takayanagi, T.; Kimura, A.; Matsui, H.
    Evaluation of subsite affinities of isomalto-dextranase from Arthrobacter globiformis (2002), J. Appl. Glycosci., 49, 123-127.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.94 additional information no inhibitors are isopanose and maltotriose Arthrobacter globiformis

Organism

EC Number Organism UniProt Comment Textmining
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 isomaltoheptaose + H2O
-
 Arthrobacter globiformis ?
-
 ?
3.2.1.94 isomaltohexaose + H2O
-
 Arthrobacter globiformis ?
-
 ?
3.2.1.94 isomaltooctaose + H2O
-
 Arthrobacter globiformis ?
-
 ?
3.2.1.94 isomaltopentaose + H2O
-
 Arthrobacter globiformis ?
-
 ?
3.2.1.94 isomaltotetraose + H2O
-
 Arthrobacter globiformis ?
-
 ?
3.2.1.94 isomaltotriose + H2O
-
 Arthrobacter globiformis alpha-isomaltose + D-glucose
-
 ?
3.2.1.94 additional information enzyme also hydrolyzes oligosaccharides with alpha-isomaltosyl unit in their non-reducing ends, no substrates are isopanose and maltotriose Arthrobacter globiformis ?
-
 ?