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Literature summary for 3.2.1.33 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

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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-
-

Purification (Commentary)

Purification (Comment) Organism
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Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
muscle
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Oryctolagus cuniculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-(1-6)-glucosyl cyclohexaamylose + H2O 6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin Oryctolagus cuniculus cyclohexaamylose + D-glucose alpha-Schardinger dextrin r
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
beta-amylase limit dextrin + H2O beta-dextrin Oryctolagus cuniculus limit dextrin + D-glucose reverse reaction: glucose incorporation into beta-limit dextrin r
D-glucose + maltooligosaccharide
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Oryctolagus cuniculus maltooligosaccharide branched r
glycogen + H2O reverse reaction: incorporation of glucose into glycogen Oryctolagus cuniculus glycogen + D-glucose
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r

pH Optimum

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