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Literature summary for 3.2.1.33 extracted from

  • Min-Ho, L.; Hyung-Nam, S.; Ji-Eun, C.; Lan, T.P.; Sunghoon, P.; Jong-Tae, P.; Eui-Jeon, W.
    Association of bi-functional activity in the N-terminal domain of glycogen debranching enzyme (2014), Biochem. Biophys. Res. Commun., 445, 107-112.
    View publication on PubMed
Search for more literature for 3.2.1.33

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3-RIL) cells Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
 x * 70000, SDS-PAGE Saccharomyces cerevisiae
640000
-
 gel filtration Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae D349
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and gel filtration Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose-beta-cyclodextrin + H2O most substrate is hydrolysed at 1 h and completely degraded at 5 h Saccharomyces cerevisiae D-glucose + beta-cyclodextrin
-
 ?
D-glucose-beta-cyclodextrin + H2O most substrate is hydrolysed at 1 h and completely degraded at 5 h Saccharomyces cerevisiae D349 D-glucose + beta-cyclodextrin
-
 ?

Subunits

Subunits Comment Organism
? x * 70000, SDS-PAGE Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
alpha-1,6-glucosidase
-
 Saccharomyces cerevisiae
GDE
-
 Saccharomyces cerevisiae
glycogen debranching enzyme the enzyme shows alpha-1,6-glucosidase activity with the C-terminal domain Saccharomyces cerevisiae