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Literature summary for 2.7.1.1 extracted from

  • Romero, C.S.; Olmo, R.; Teijon, C.; Blanco, M.D.; Teijon, J.M.; Romero, A.
    Structural and functional implications of the hexokinase-nickel interaction (2005), J. Inorg. Biochem., 99, 2395-2402.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Ni2+ competitive versus ATP via replacement of Mg2+, noncompetitive versus D-glucose via a cysteine residue proximal to the D-glucose binding site, enzyme-nickel interactions with positive cooperativity via histidine residues, no saturation is reached, nickel binding induces conformational changes in the secondary structure of the enzyme modifying the monomer/dimer equilibrium and decreasing the activity, overview Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-glucose Saccharomyces cerevisiae
-
ADP + D-glucose 6-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + D-hexose = ADP + D-hexose 6-phosphate catalytic residues in the D-glucose binding site are Glu269, Glu302, and Asp211 Saccharomyces cerevisiae

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer at lower Ni2+ concentration Saccharomyces cerevisiae
monomer at very high Ni2+ concentration Saccharomyces cerevisiae
More enzyme-nickel interactions modify the monomer/dimer equilibrium, overview Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.87
-
Ni2+ pH 7.6, 37°C, versus ATP Saccharomyces cerevisiae
9.97
-
Ni2+ pH 7.6, 37°C, versus D-glucose Saccharomyces cerevisiae