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Literature summary extracted from

  • Gillard, B.K.; Nelson, T.E.
    Amylo-1,6-glucosidase/4-alpha-glucanotransferase: use of reversible substrate model inhibitors to study the binding and active sites of rabbit muscle debranching enzyme (1977), Biochemistry, 16, 3978-3987.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.33 1,4-diaminobutane putrescine, glycogen debranching enzyme, slight inhibition Oryctolagus cuniculus
3.2.1.33 2,2-bis(hydroxymethyl)-2,2',2''-nitrilotriethanol Bis-Tris, reversible inhibitor; noncompetitive with glycogen phosphorylase limit dextrin, competitive with glucose Oryctolagus cuniculus
3.2.1.33 2-(2-hydroxyethylamino)-2-hydroxymethyl-1,3-propanediol hydroxyethyltris Oryctolagus cuniculus
3.2.1.33 2-amino-1,3-propandiol
-
 Oryctolagus cuniculus
3.2.1.33 2-amino-2-methyl-1,3-propanediol
-
 Oryctolagus cuniculus
3.2.1.33 2-hydroxyethyl-3-hydroxypropylamine HEPA, glycogen debranching enzyme Oryctolagus cuniculus
3.2.1.33 3-aminopropyl-2-hydroxyethylamine DAPH, glycogen debranching enzyme Oryctolagus cuniculus
3.2.1.33 5-amino-D-glucose nojirimycin, potent inhibitor, noncompetitive Oryctolagus cuniculus
3.2.1.33 5-thio-D-glucose slight inhibition Oryctolagus cuniculus
3.2.1.33 Amine noncompetitive with glycogen phosphorylase limit dextrin, competitive with glucose; polyhydroxyamines, mechanism of inhibition; protonated, hydroxylalkyl-substituted, noncompetitive, mechanism of inhibition Oryctolagus cuniculus
3.2.1.33 cyclohexaamylose alpha-Schardinger dextrin, debranching enzyme, competitive inhibitor Oryctolagus cuniculus
3.2.1.33 D-glucono-1,5-lactone glycogen debranching enzyme, noncompetitive with glycogen phosphorylase limit dextrin, competitive with glucose Oryctolagus cuniculus
3.2.1.33 ethylamine slight inhibition Oryctolagus cuniculus
3.2.1.33 glycogen competitive Oryctolagus cuniculus
3.2.1.33 m-erythritol noncompetitive Oryctolagus cuniculus
3.2.1.33 additional information inhibition mechanism; no inhibition by dithioerythritol, dithiothreitol, cadaverine, spermidine, spermine, D,L-threitol, 1-thio-beta-D-glucose Oryctolagus cuniculus
3.2.1.33 N,N'-bis(tris[hydroxymethyl]methyl)-1,3-diaminopropane bis(tris)propane, noncompetitive Oryctolagus cuniculus
3.2.1.33 Tris noncompetitive; Tris analogues Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.33 additional information
-
 additional information kinetic data Oryctolagus cuniculus
3.2.1.33 additional information
-
 additional information kinetic mechanism Oryctolagus cuniculus
3.2.1.33 43
-
 D-glucose
-
 Oryctolagus cuniculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.33 160000 170000
-
 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 Oryctolagus cuniculus phi-dextrin ?
-
 ?
3.2.1.33 glycogen phosphorylase-limit dextrin + H2O Oryctolagus cuniculus total degradation of glycogen is accomplished by the combined action of glycogen phosphorylase and glycogen debranching enzyme ?
-
 ?

Organism

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

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.33 6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O = D-glucose + cyclomaltoheptaose mechanism Oryctolagus cuniculus
a
3.2.1.33 6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O = D-glucose + cyclomaltoheptaose thermodynamic data Oryctolagus cuniculus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.33 muscle skeletal 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 6.5 8.9
-
 Oryctolagus cuniculus

Storage Stability

EC Number Storage Stability Organism
3.2.1.33 4°C, 50 mM Tris, 5 mM EDTA, 1 mM dithiothreitol, pH 7.2 Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.33 63-alpha-glucosyl maltotetraose + H2O branched pentasaccharide "fast B5" Oryctolagus cuniculus maltotetraose + D-glucose
-
 r
3.2.1.33 alpha-(1-6)-glucosyl cyclohexaamylose + H2O 6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin Oryctolagus cuniculus cyclohexaamylose + D-glucose
-
 r
3.2.1.33 glycogen + H2O slowly hydrolyzed Oryctolagus cuniculus 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 phi-dextrin Oryctolagus cuniculus limit dextrin + D-glucose
-
 r
3.2.1.33 glycogen phosphorylase-limit dextrin + H2O phi-dextrin Oryctolagus cuniculus ?
-
 ?
3.2.1.33 glycogen phosphorylase-limit dextrin + H2O total degradation of glycogen is accomplished by the combined action of glycogen phosphorylase and glycogen debranching enzyme Oryctolagus cuniculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.33 monomer
-
 Oryctolagus cuniculus

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 Oryctolagus cuniculus