The enzyme catalyses the hydrolysis of alpha-1,6-glucosidic linkages from the non-reducing end of its substrate. Unlike EC 3.2.1.10, oligo-1,6-glucosidase, the enzyme inverts the anomeric configuration of the released residue. The enzyme can also act on panose and maltotriose at a lower rate.
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The expected taxonomic range for this enzyme is: Kribbella flavida
The enzyme catalyses the hydrolysis of alpha-1,6-glucosidic linkages from the non-reducing end of its substrate. Unlike EC 3.2.1.10, oligo-1,6-glucosidase, the enzyme inverts the anomeric configuration of the released residue. The enzyme can also act on panose and maltotriose at a lower rate.
enzyme effectively hydrolyzes isomaltose with liberation of beta-glucose, but displays low or no activity toward cyclobis-(1->6)-alpha-nigerosyl and the general GH15 enzyme substrates such as maltose, soluble starch, or dextran
enzyme effectively hydrolyzes isomaltose with liberation of beta-glucose, but displays low or no activity toward cyclobis-(1->6)-alpha-nigerosyl and the general GH15 enzyme substrates such as maltose, soluble starch, or dextran
enzyme effectively hydrolyzes isomaltose with liberation of beta-D-glucose, but displays low or no activity toward cyclobis-(1->6)-alpha-nigerosyl and the general GH15 enzyme substrates such as maltose, soluble starch, or dextran
enzyme effectively hydrolyzes isomaltose with liberation of beta-D-glucose, but displays low or no activity toward cyclobis-(1->6)-alpha-nigerosyl and the general GH15 enzyme substrates such as maltose, soluble starch, or dextran
enzyme effectively hydrolyzes isomaltose with liberation of beta-glucose, but displays low or no activity toward cyclobis-(1->6)-alpha-nigerosyl and the general GH15 enzyme substrates such as maltose, soluble starch, or dextran
enzyme effectively hydrolyzes isomaltose with liberation of beta-D-glucose, but displays low or no activity toward cyclobis-(1->6)-alpha-nigerosyl and the general GH15 enzyme substrates such as maltose, soluble starch, or dextran
enzyme effectively hydrolyzes isomaltose with liberation of beta-glucose, but displays low or no activity toward cyclobis-(1->6)-alpha-nigerosyl and the general GH15 enzyme substrates such as maltose, soluble starch, or dextran
enzyme effectively hydrolyzes isomaltose with liberation of beta-glucose, but displays low or no activity toward cyclobis-(1->6)-alpha-nigerosyl and the general GH15 enzyme substrates such as maltose, soluble starch, or dextran
enzyme effectively hydrolyzes isomaltose with liberation of beta-glucose, but displays low or no activity toward cyclobis-(1->6)-alpha-nigerosyl and the general GH15 enzyme substrates such as maltose, soluble starch, or dextran
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Enzyme Nomenclature
3.2.1.205 isomaltose glucohydrolase
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