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Literature summary extracted from

  • Nakayama, A.; Yamamoto, K.; Tabata, S.
    Identification of the catalytic residues of bifunctional glycogen debranching enzyme (2001), J. Biol. Chem., 276, 28824-28828.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.33 D1086N loss of glucosidase activity Saccharomyces cerevisiae
3.2.1.33 D1147N loss of glucosidase activity Saccharomyces cerevisiae
3.2.1.33 D535N loss of transferase activity Saccharomyces cerevisiae
3.2.1.33 D670N loss of transferase activity Saccharomyces cerevisiae
3.2.1.33 E564Q loss of transferase activity Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.33 15.9
-
 6-O-alpha-D-glucosyl cyclomaltoheptaose mutant E564Q, pH 6.5, 37°C Saccharomyces cerevisiae
3.2.1.33 16.3
-
 6-O-alpha-D-glucosyl cyclomaltoheptaose wild type, pH 6.5, 37°C Saccharomyces cerevisiae
3.2.1.33 16.6
-
 6-O-alpha-D-glucosyl cyclomaltoheptaose mutant D535N, pH 6.5, 37°C Saccharomyces cerevisiae
3.2.1.33 19.3
-
 6-O-alpha-D-glucosyl cyclomaltoheptaose mutant D670N, pH 6.5, 37°C Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.33 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.33 6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O
-
 Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.33 More transferase and glucosidase activities are independent and located at different sites of the polypeptide chain Saccharomyces cerevisiae