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Literature summary for 5.1.3.15 extracted from

  • Wurster, B.; Hess, B.
    Glucose-6-phosphate 1-epimerase from bakers' yeast: purification, properties and possible biological function (1974), Hoppe-Seyler's Z. Physiol. Chem., 355, 255-265.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Cl-
-
Saccharomyces cerevisiae
EDTA
-
Saccharomyces cerevisiae
additional information in contrast to glucosephosphate isomerase, glucose-6-phosphate 1-epimerase is not inhibited by D-erythrose 4-phosphate and D-gluconate 6-phosphate Saccharomyces cerevisiae
NADP+
-
Saccharomyces cerevisiae
phosphate
-
Saccharomyces cerevisiae
SO42-
-
Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-D-glucose 6-phosphate
-
Saccharomyces cerevisiae beta-D-glucose 6-phosphate
-
?
additional information enzyme catalyzes to a small extent the anomerization of D-glucose. The activity constant for D-glucose is 70000 times smaller than the activity constant for D-glucose 6-phosphate Saccharomyces cerevisiae ?
-
?