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Literature summary 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

Inhibitors

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

Organism

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.33 liver
-
 Oryctolagus cuniculus
-
3.2.1.33 muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.33 63-alpha-glucosyl maltopentaose + H2O
-
 Oryctolagus cuniculus maltopentaose + D-glucose
-
 r
3.2.1.33 63-alpha-glucosyl maltotetraose + H2O
-
 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 alpha-Schardinger dextrin 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 additional information
-
 Oryctolagus cuniculus ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.33 additional information
-
 2 enzymes: one with an acid and one with a neutral pH-optimum Oryctolagus cuniculus
3.2.1.33 6
-
 substrate: glycogen phosphorylase limit dextrin, citrate /phosphate buffer Oryctolagus cuniculus
3.2.1.33 7.6
-
 citrate buffer Oryctolagus cuniculus