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Literature summary for 3.2.1.33 extracted from

  • Nelson, T.E.; Kolb, E.; Larner, J.
    Purification and properties of rabbit muscle amylo-1,6-glucosidase-oligo-1,4->1,4-transferase (1969), Biochemistry, 8, 1419-1428.
    View publication on PubMed
Search for more literature for 3.2.1.33

Inhibitors

Inhibitors Comment Organism Structure
2-(N-morpholino)ethanesulfonic acid
-
 Oryctolagus cuniculus
Amine protonated, hydroxylalkyl-substituted, noncompetitive, mechanism of inhibition Oryctolagus cuniculus
cationic buffer
-
 Oryctolagus cuniculus
choline very poor inhibitor Oryctolagus cuniculus
diethanolamine
-
 Oryctolagus cuniculus
ethanolamine
-
 Oryctolagus cuniculus
ethylamine
-
 Oryctolagus cuniculus
glycylglycine no inhibition at 0.01 or 0.05 M Oryctolagus cuniculus
hydroxylamine
-
 Oryctolagus cuniculus
imidazole
-
 Oryctolagus cuniculus
additional information inhibition mechanism Oryctolagus cuniculus
N-2-Hydroxyethylpiperazine-N'-2-ethanesulfonic acid slight inhibition Oryctolagus cuniculus
N-Tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid slight inhibition Oryctolagus cuniculus
NH4+ slight inhibition Oryctolagus cuniculus
taurine slight inhibition Oryctolagus cuniculus
triethylamine very poor inhibitor Oryctolagus cuniculus
Tris
-
 Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Oryctolagus cuniculus
0.063
-
 glycogen phosphorylase limit dextrin
-
 Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
glycogen debranching enzyme 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
8.3
-
-
 Oryctolagus cuniculus
9.5
-
-
 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
alpha-(1-6)-glucosyl cyclohexaamylose + H2O 6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin Oryctolagus cuniculus cyclohexaamylose + D-glucose alpha-Schardinger dextrin r
amylopectin + H2O very poor substrate Oryctolagus cuniculus amylopectin + D-glucose
-
 r
glycogen + H2O rabbit liver glycogen: slowly 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

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
6
-
 phosphate-citrate buffer Oryctolagus cuniculus
6.6
-
 anionic buffer, substrate: glycogen phosphorylase limit dextrin Oryctolagus cuniculus
6.6
-
 imidazole buffer Oryctolagus cuniculus
7.2
-
 cationic buffer, substrate: glycogen phosphorylase limit dextrin Oryctolagus cuniculus

pH Range

pH Minimum pH Maximum Comment Organism
5 8
-
 Oryctolagus cuniculus