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Literature summary for 3.2.1.94 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)

Cloned (Comment) Organism
expressed in Escherichia coli Arthrobacter globiformis

Inhibitors

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Arthrobacter globiformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
pullulan + H2O enzyme also has a weak isopullulanase activity Arthrobacter globiformis isopanose
-
?

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3
-
-
Arthrobacter globiformis