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Literature summary for 3.2.1.33 extracted from

  • Taylor, P.M.; Whelan, W.J.
    Rabbit muscle amylo-1,6-glucosidase: properties and evidence of heterogeneity (1968), Control of Glycogen Metabolism, Proc. FEBS 4th Meeting, Oslo, 1967 (Whelan, W. J. , ed. ), , 101-114.
No PubMed abstract available
Search for more literature for 3.2.1.33

Inhibitors

Inhibitors Comment Organism Structure
glycylglycine inhibits at acidic pH Oryctolagus cuniculus
phosphate buffer, inhibits at neutral pH Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
 2 enzymes: acidic and neutral
-

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
63-alpha-glucosyl maltopentaose + H2O
-
 Oryctolagus cuniculus maltopentaose + D-glucose
-
 r
63-alpha-glucosyl maltotetraose + H2O
-
 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
glycogen + H2O reverse reaction: incorporation of glucose into glycogen Oryctolagus cuniculus glycogen + D-glucose
-
 r
glycogen phosphorylase-limit dextrin + H2O phi-dextrin Oryctolagus cuniculus limit dextrin + D-glucose
-
 r
additional information
-
 Oryctolagus cuniculus ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 2 enzymes: one with an acid and one with a neutral pH-optimum Oryctolagus cuniculus
6
-
 substrate: glycogen phosphorylase limit dextrin, citrate /phosphate buffer Oryctolagus cuniculus
7.6
-
 citrate buffer Oryctolagus cuniculus