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Literature summary for 2.7.1.1 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
Search for more literature for 2.7.1.1

Activating Compound

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

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

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

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + ATP
-
 Saccharomyces cerevisiae ADP + D-glucose 6-phosphate
-
 ?
D-mannose + ATP
-
 Saccharomyces cerevisiae ADP + D-mannose 6-phosphate
-
 ?
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]

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

pH Optimum

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

Cofactor

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