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Literature summary for 2.7.1.1 extracted from

  • Molnes, J.; Teigen, K.; Aukrust, I.; Bjorkhaug, L.; Sovik, O.; Flatmark, T.; Njolstad, P.R.
    Binding of ATP at the active site of human pancreatic glucokinase--nucleotide-induced conformational changes with possible implications for its kinetic cooperativity (2011), FEBS J., 278, 2372-2386.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a GST-tagged fusion protein Homo sapiens

Protein Variants

Protein Variants Comment Organism
L146R mutant shows a 100fold reduced kcat and a 40fold increase in [S]0.5 value for D-glucose. Km (ATP) is slightly increased compared to wild-type Homo sapiens
T228M mutant shows a 9000fold reduced activity Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
 ATP wild-type, 37°C, pH not specified in the puclication. Kinetic constants at high and low concentrations of the fixed substrate: 0.5 mM D-glucose Homo sapiens
0.16
-
 ATP wild-type, 37°C, pH not specified in the puclication Homo sapiens
0.16
-
 ATP wild-type, 37°C, pH not specified in the puclication. Kinetic constants at high and low concentrations of the fixed substrate: 60 mM D-glucose Homo sapiens
0.24
-
 ATP mutant L146R, 37°C, pH not specified in the puclication Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
ATP + D-glucose = ADP + D-glucose 6-phosphate using intrinsic tryptophan fluorescence a conformational change induced by the binding of adenine nucleotides to human pancreatic glucokinase is determined. The molecular dynamic simulations indicate that the binding triggers molecular motion of the flexible surface /active site loop and partial closure of the interdomain active site cleft. The modelled structure of the hGK-ATP binary complex shows the residue contacts involved in ATP binding at the active site Homo sapiens
a

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
glucokinase
-
 Homo sapiens
hGK
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.007
-
 D-glucose mutant T228M, 37°C, pH not specified in the puclication Homo sapiens
0.61
-
 ATP mutant L146R, 37°C, pH not specified in the puclication Homo sapiens
0.7
-
 ATP wild-type, 37°C, pH not specified in the puclication. Kinetic constants at high and low concentrations of the fixed substrate: 0.5 mM D-glucose Homo sapiens
0.77
-
 D-glucose mutant L146R, 37°C, pH not specified in the puclication Homo sapiens
67.6
-
 D-glucose wild-type, 37°C, pH not specified in the puclication Homo sapiens
68.4
-
 ATP wild-type, 37°C, pH not specified in the puclication Homo sapiens
68.4
-
 ATP wild-type, 37°C, pH not specified in the puclication. Kinetic constants at high and low concentrations of the fixed substrate: 60 mM D-glucose Homo sapiens