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Literature summary for 3.2.1.33 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
Search for more literature for 3.2.1.33

Protein Variants

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

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

Subunits

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