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Literature summary extracted from

  • Lee, E.Y.C.; Carter, J.H.
    Amylo-1,6-glucosidase/1,4-alpha-glucan: 1,4-alpha-glucan 4-alpha-glycosyltransferase: specificity toward polysaccharide substrates (1973), Arch. Biochem. Biophys., 154, 636-641.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.33 0.74
-
glycogen phosphorylase limit dextrin phi-dextrin from shellfish glycogen Oryctolagus cuniculus
3.2.1.33 1.6
-
glycogen phosphorylase limit dextrin phi-dextrin from shellfish glycogen Saccharomyces cerevisiae
3.2.1.33 3.8
-
beta-amylase limit dextrin beta-dextrin from shellfish glycogen Saccharomyces cerevisiae
3.2.1.33 4.3
-
amylopectin beta-dextrin
-
Saccharomyces cerevisiae
3.2.1.33 7.2
-
beta-amylase limit dextrin beta-dextrin from shellfish glycogen Oryctolagus cuniculus
3.2.1.33 11
-
amylopectin beta-dextrin
-
Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.33 glycogen phosphorylase-limit dextrin + H2O Saccharomyces cerevisiae phi-dextrin ?
-
?
3.2.1.33 glycogen phosphorylase-limit dextrin + H2O Oryctolagus cuniculus phi-dextrin ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.33 Oryctolagus cuniculus
-
-
-
3.2.1.33 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.33 glycogen debranching enzyme Saccharomyces cerevisiae
3.2.1.33 glycogen debranching enzyme Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.33 muscle
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.33 6
-
-
Saccharomyces cerevisiae
3.2.1.33 7.6
-
-
Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.33 amylopectin + H2O very poor substrate Oryctolagus cuniculus amylopectin + D-glucose partially debranched r
3.2.1.33 amylopectin + H2O phi-dextrin, beta-dextrin and phi-beta-dextrin from amylopectin Saccharomyces cerevisiae amylopectin + D-glucose partially debranched r
3.2.1.33 amylopectin + H2O phi-dextrin, beta-dextrin and phi-beta-dextrin from amylopectin Oryctolagus cuniculus amylopectin + D-glucose partially debranched r
3.2.1.33 amylopectin beta-dextrin + H2O
-
Saccharomyces cerevisiae ?
-
?
3.2.1.33 amylopectin beta-dextrin + H2O
-
Oryctolagus cuniculus ?
-
?
3.2.1.33 amylose + H2O
-
Saccharomyces cerevisiae ?
-
r
3.2.1.33 amylose + H2O
-
Oryctolagus cuniculus ?
-
r
3.2.1.33 beta-amylase limit dextrin + H2O beta-dextrin Saccharomyces cerevisiae limit dextrin + D-glucose
-
r
3.2.1.33 beta-amylase limit dextrin + H2O beta-dextrin Oryctolagus cuniculus limit dextrin + D-glucose
-
r
3.2.1.33 glycogen + H2O rabbit liver glycogen: very poor substrate, shellfish glycogen: not a substrate Oryctolagus cuniculus glycogen + D-glucose
-
r
3.2.1.33 glycogen + H2O reverse reaction: synthesis of (1, 6)-bound side chains, reincorporation of glucose into polysaccharide Saccharomyces cerevisiae glycogen + D-glucose
-
r
3.2.1.33 glycogen + H2O reverse reaction: synthesis of (1, 6)-bound side chains, reincorporation of glucose into polysaccharide Oryctolagus cuniculus glycogen + D-glucose
-
r
3.2.1.33 glycogen + H2O native glycogen from shellfish and rabbit liver Saccharomyces cerevisiae glycogen + D-glucose
-
r
3.2.1.33 glycogen + H2O reverse reaction: incorporation of glucose into glycogen Saccharomyces cerevisiae glycogen + D-glucose
-
r
3.2.1.33 glycogen + H2O reverse reaction: incorporation of glucose into glycogen Oryctolagus cuniculus glycogen + D-glucose
-
r
3.2.1.33 glycogen phosphorylase limit dextrin + H2O
-
Saccharomyces cerevisiae ?
-
?
3.2.1.33 glycogen phosphorylase limit dextrin + H2O
-
Oryctolagus cuniculus ?
-
?
3.2.1.33 glycogen phosphorylase-limit dextrin + H2O phi-dextrin Saccharomyces cerevisiae limit dextrin + D-glucose
-
r
3.2.1.33 glycogen phosphorylase-limit dextrin + H2O phi-dextrin Oryctolagus cuniculus limit dextrin + D-glucose
-
r
3.2.1.33 glycogen phosphorylase-limit dextrin + H2O phi-dextrin Saccharomyces cerevisiae ?
-
?
3.2.1.33 glycogen phosphorylase-limit dextrin + H2O phi-dextrin Oryctolagus cuniculus ?
-
?
3.2.1.33 additional information substrate specificities Saccharomyces cerevisiae ?
-
?
3.2.1.33 additional information substrate specificities Oryctolagus cuniculus ?
-
?
3.2.1.33 phosphorylase beta-amylase limit dextrin + H2O limit dextrin, beta-phi-dextrin, derived from the action of beta-amylase on the phosphorylase limit dextrin Saccharomyces cerevisiae limit dextrin + D-glucose
-
r
3.2.1.33 phosphorylase beta-amylase limit dextrin + H2O limit dextrin, beta-phi-dextrin, derived from the action of beta-amylase on the phosphorylase limit dextrin Oryctolagus cuniculus limit dextrin + D-glucose
-
r

Synonyms

EC Number Synonyms Comment Organism
3.2.1.33 glycogen debranching system EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system Saccharomyces cerevisiae
3.2.1.33 glycogen debranching system EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system Oryctolagus cuniculus