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Literature summary for 3.2.1.33 extracted from

  • Brown, D.H.; Gordon, R.B.; Illingworth Brown, B.
    Studies on the structure and mechanism of action of the glycogen debranching enzymes of muscle and liver (1973), Ann. N. Y. Acad. Sci., 210, 238-253.
    View publication on PubMed
Search for more literature for 3.2.1.33

General Stability

General Stability Organism
stable in 2 M urea, irreversible denaturation with higher concentrations, 3 M, of urea Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
guanidine muscle and liver enzyme: inhibition at very low concentrations Oryctolagus cuniculus
SDS irreversible inhibition by less than 0.1% SDS Oryctolagus cuniculus
Urea muscle enzyme: reversible 95% inhibition by 2 M urea, with higher concentration, 3 M urea: time-dependent irreversible denaturation, liver enzyme: reversible 57% inhibition by 2 M urea Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.45
-
 63-alpha-glucosyl maltotetraose branched pentasaccharide "fast B5", muscle enzyme Oryctolagus cuniculus
5.6
-
 63-alpha-maltotriosyl maltotetraose branched heptasaccharide B7, muscle enzyme Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
-
 Oryctolagus cuniculus
169200
-
 glycogen debranching enzyme, muscle enzyme, equilibrium ultracentrifugation Oryctolagus cuniculus
170000
-
 glycogen debranching enzyme, muscle enzyme, sucrose density gradient centrifugation Oryctolagus cuniculus
179300
-
 glycogen debranching enzyme, liver enzyme, sucrose density gradient centrifugation Oryctolagus cuniculus
267000 279000 glycogen debranching enzyme can probably form a complex with one or more other soluble proteins Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
glycogen debranching enzyme Oryctolagus cuniculus
muscle and liver Oryctolagus cuniculus

Reaction

Reaction Comment Organism Reaction ID
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O = D-glucose + cyclomaltoheptaose mechanism Oryctolagus cuniculus
a

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Oryctolagus cuniculus
-
muscle skeletal Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.5
-
 liver enzyme Oryctolagus cuniculus
8 10 muscle enzyme Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
63-alpha-glucosyl maltotetraose + H2O branched pentasaccharide "fast B5" Oryctolagus cuniculus maltotetraose + D-glucose
-
 r
63-alpha-maltotriosyl maltotetraose + H2O branched heptasaccharide B7 Oryctolagus cuniculus ?
-
 ?
glycogen phosphorylase-limit dextrin + H2O
-
 Oryctolagus cuniculus limit dextrin + D-glucose
-
 r

Subunits

Subunits Comment Organism
monomer 1 * 170000, glycogen debranching enzyme, SDS-PAGE 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