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Literature summary for 3.2.1.33 extracted from

  • Nelson, T.E.; Kolb, E.; Larner, J.
    Reinvestigation of the pH optimum in terms of the action and properties of rabbit muscle amylo-1,6-glucosidase-oligo-1,4 -> 1,4-transferase (1968), Biochim. Biophys. Acta, 167, 212-215.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Tris
-
Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
glycogen debranching enzyme Oryctolagus cuniculus

Reaction

Reaction Comment Organism Reaction ID
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O = D-glucose + cyclomaltoheptaose mechanism Oryctolagus cuniculus
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O = D-glucose + cyclomaltoheptaose alpha-(1->6) linkage can be synthesized in the absence of polysaccharide Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.5 8.3
-
Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 D-glucose
-
Oryctolagus cuniculus 6-O-alpha-D-glucosyl-D-glucose + H2O isomaltose r
63-alpha-glucosyl maltotetraose + H2O branched pentasaccharide "fast B5" Oryctolagus cuniculus maltotetraose + D-glucose
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
-
Oryctolagus cuniculus cyclohexaamylose + D-glucose
-
r
glycogen + H2O reverse reaction: synthesis of (1, 6)-bound side chains, reincorporation of glucose into polysaccharide Oryctolagus cuniculus glycogen + D-glucose
-
r
glycogen phosphorylase-limit dextrin + H2O
-
Oryctolagus cuniculus limit dextrin + D-glucose
-
r

Synonyms

Synonyms Comment Organism
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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
pH-optimum depends on type of buffer Oryctolagus cuniculus
additional information
-
pH optimum is the same in both degradative and synthetic directions and optimum is shifted and inhibited by Tris in the same manner in both directions Oryctolagus cuniculus
6.6
-
anionic buffer, substrate: glycogen phosphorylase limit dextrin Oryctolagus cuniculus
7.2
-
cationic buffer, substrate: glycogen phosphorylase limit dextrin Oryctolagus cuniculus