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Literature summary for 3.2.1.33 extracted from

  • Liu, W.; Madsen, N.B.; Braun, C.; Withers, S.G.
    Reassessment of the catalytic mechanism of glycogen debranching enzyme (1991), Biochemistry, 30, 1419-1424.
    View publication on PubMed
Search for more literature for 3.2.1.33

Inhibitors

Inhibitors Comment Organism Structure
2,2-bis(hydroxymethyl)-2,2',2''-nitrilotriethanol 10 mM: 97% inhibition; Bis-Tris, reversible inhibitor Oryctolagus cuniculus
2-deoxy-2-fluoro-alpha-glucosyl fluoride very poor inhibitor, 56 mM: 17% inhibition Oryctolagus cuniculus
deoxynojirimycin reversible, specific inhibitor Oryctolagus cuniculus
methanediimine carbodiimide in the presence of an amine inhibits glycogen debranching enzyme, transferase activity is inhibited, amylo-1,6-glucosidase , hydrolysis of alpha-glucosyl fluoride, is unaffected by carbodiimide. Slow inactivation of glucosidase activity as measured by [14C]glucose incorporation into glycogen Oryctolagus cuniculus
additional information
-
 Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic data Oryctolagus cuniculus
0.063
-
 glycogen phosphorylase limit dextrin phi-dextrin Oryctolagus cuniculus
2.8
-
 alpha-glucosyl fluoride
-
 Oryctolagus cuniculus
8.1
-
 alpha-glucosyl fluoride with 9.6% glycogen Oryctolagus cuniculus
32
-
 D-glucose in the presence of glycogen Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycogen phosphorylase-limit dextrin + H2O 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
a
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O = D-glucose + cyclomaltoheptaose stereochemistry Oryctolagus cuniculus
a

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
11
-
-
 Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-2-fluoro-alpha-D-glucosyl fluoride poor substrate Oryctolagus cuniculus ?
-
 ?
alpha-(1-6)-glucosyl cyclohexaamylose + H2O 6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin Oryctolagus cuniculus cyclohexaamylose + D-glucose
-
 r
alpha-D-glucosyl fluoride in absence or presence of glycogen or polysaccharide Oryctolagus cuniculus fluoride + D-glucose
-
 ?
glycogen + H2O reverse reaction: incorporation of glucose into glycogen Oryctolagus cuniculus glycogen + D-glucose
-
 r
glycogen phosphorylase limit dextrin + H2O
-
 Oryctolagus cuniculus ?
-
 ?
glycogen phosphorylase-limit dextrin + H2O
-
 Oryctolagus cuniculus limit dextrin + D-glucose
-
 r
glycogen phosphorylase-limit dextrin + H2O
-
 Oryctolagus cuniculus ?
-
 ?

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