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Literature summary extracted from

  • Stark, J.R.; Thambyrajah, V.
    Studies on the reverse action of amylo-1,6-glucosidase (1970), Biochem. J., 120, 17P-18P.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.33 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.33
-
 Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
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 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 beta-amylase limit dextrin + H2O reverse reaction: glucose incorporation into beta-limit dextrin Oryctolagus cuniculus limit dextrin + D-glucose reverse reaction: glucose incorporation into beta-limit dextrin r
3.2.1.33 beta-amylase limit dextrin + H2O beta-dextrin Oryctolagus cuniculus limit dextrin + D-glucose reverse reaction: glucose incorporation into beta-limit dextrin r
3.2.1.33 D-glucose + maltooligosaccharide
-
 Oryctolagus cuniculus maltooligosaccharide branched r
3.2.1.33 glycogen + H2O reverse reaction: incorporation of glucose into glycogen Oryctolagus cuniculus glycogen + D-glucose
-
 r

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.33 additional information
-
 reverse action of amylo-1,6-glucosidase: pH optimum depends on different acceptor substrates Oryctolagus cuniculus