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Literature summary for 3.2.1.94 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
Search for more literature for 3.2.1.94

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isomaltoheptaose + H2O
-
 Arthrobacter globiformis ?
-
 ?
isomaltohexaose + H2O
-
 Arthrobacter globiformis ?
-
 ?
isomaltooctaose + H2O
-
 Arthrobacter globiformis ?
-
 ?
isomaltopentaose + H2O
-
 Arthrobacter globiformis ?
-
 ?
isomaltotetraose + H2O
-
 Arthrobacter globiformis ?
-
 ?
isomaltotriose + H2O
-
 Arthrobacter globiformis alpha-isomaltose + D-glucose
-
 ?
additional information enzyme also hydrolyzes oligosaccharides with alpha-isomaltosyl unit in their non-reducing ends, no substrates are isopanose and maltotriose Arthrobacter globiformis ?
-
 ?