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Literature summary for 3.2.1.33 extracted from

  • Makino, Y.; Omichi, K.
    Purification of glycogen debranching enzyme from porcine brain: evidence for glycogen catabolism in the brain (2006), Biosci. Biotechnol. Biochem., 70, 907-915.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
D-glucose 10% inhibition by 10 mM, 50% inhibition by 50 mM Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
170000
-
gel filtration Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information activity with glycogen, soluble starch, amylopektin and pullulan is less than 1% of the activity with phosphorylase limit dextrin Sus scrofa ?
-
?
phosphorylase limit dextrin + H2O the purified enzyme has both maltooligosaccharide transferase and amylo-1,6-glucosidase activities within a single polypeptide chain, and the combination of these two activities removes the branches of phosphorylase limit dextrin Sus scrofa ?
-
?

Synonyms

Synonyms Comment Organism
amylo-1,6-glucosidase
-
Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
Sus scrofa

pH Range

pH Minimum pH Maximum Comment Organism
5 7 pH 5.0: about 25% of maximal activity, pH 5.5: about 70% of maximal activity, pH 6.5: about 60% of maximal activity, pH 7.0: about 20% of maximal activity Sus scrofa