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Literature summary extracted from

  • Yamamoto, E.; Makino, Y.; Omichi, K.
    Active site mapping of amylo-alpha-1,6-glucosidase in porcine liver glycogen debranching enzyme using fluorogenic 6-O-alpha-glucosyl-maltooligosaccharides (2007), J. Biochem., 141, 627-634.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.33 Sus scrofa
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-
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.33 liver
-
Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.33 Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-(Glc-alpha-1,6)Glc-alpha-1,4-Glc-alpha-1,4-Glc + H2O the substrate is hydrolyzed most rapidly Sus scrofa Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc + D-glucose
-
?
3.2.1.33 additional information the alpha-1,6-glycosidic linkage of dextrins (Glc-alpha-1,4)m-(Glc-alpha-1,6)Glc-alpha-1,4-(Glc-alpha-1,4)n-1-deoxy-1-[2(pyridyl)amino]-D-glucitol with m equal 0 or n equal 0 can not be hydrolyzed by the enzyme, indicating that at least the two glycosyl residues sandwiching the isomaltosyl moiety are indispensable for hydrolysis by the GDE amylo-alpha-1,6-glucosidase activity Sus scrofa ?
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?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.33 dextrin 6-alpha-glucosidase part of the glycogen debranching enzyme, hydrolyzes dextrins with the structure Glc-alpha-1,4-(Glc-alpha-1,6)Glc-alpha-1,4-Glc to D-glucose and the corresponding pyridylamino-maltooligosaccharides Sus scrofa