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Literature summary extracted from

  • Mulcahy, P.; O'Flaherty, M.; Jennings, L.; Griffin, T.
    Application of kinetic-based biospecific affinity chromatographic systems to ATP-dependent enzymes: Studies with yeast hexokinase (2002), Anal. Biochem., 309, 279-292.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.1.1 3-phosphoglycerate activates Saccharomyces cerevisiae
2.7.1.1 citrate allosteric activator Saccharomyces cerevisiae
2.7.1.1 phosphate activates Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.1 D-mannose competitive to D-glucose Saccharomyces cerevisiae

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.1 kinetic-based biospecific affinity chromatographic studies Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.1 ATP + D-hexose = ADP + D-hexose 6-phosphate random process Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.1 D-glucose + ATP
-
Saccharomyces cerevisiae ADP + D-glucose 6-phosphate
-
?
2.7.1.1 D-mannose + ATP
-
Saccharomyces cerevisiae ADP + D-mannose 6-phosphate
-
?
2.7.1.1 additional information allosteric enzyme, catalyzes phosphoryl transfer from MgATP2- to the 6-OH group of a number of furanose- and pyranose-type compounds Saccharomyces cerevisiae ?
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.1 25
-
assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.1 7.5
-
assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.1 ATP activates, ATP-dependent enzyme Saccharomyces cerevisiae