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Literature summary for 2.7.1.1 extracted from

  • Marotta, D.E.; Anand, G.R.; Anderson, T.A.; Miller, S.P.; Okar, D.A.; Levitt, D.G.; Lange, A.J.
    Identification and characterization of the ATP-binding site in human pancreatic glucokinase (2005), Arch. Biochem. Biophys., 436, 23-31.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
D158A naturally occurring mutation, activity and kinetics are similar to the wild-type enzyme Homo sapiens
D78A/D158A site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Homo sapiens
G227A/D158A site-directed mutagenesis, reduced activity compared to the wild-type enzyme Homo sapiens
K102A/D158A site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme Homo sapiens
K90A/D158A site-directed mutagenesis, 2fold increased activity compared to the wild-type enzyme Homo sapiens
S336L site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Homo sapiens
S411A site-directed mutagenesis, reduced activity compared to the wild-type enzyme Homo sapiens
S411L site-directed mutagenesis, reduced activity compared to the wild-type enzyme Homo sapiens
T228A site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Homo sapiens
T228A/D158A site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme Homo sapiens
T82A site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information wild-type and mutant enzymes, cooperative/sigmoidal glucose-dependent kinetics Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ as MgATP2-, binding site structure Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-glucose Homo sapiens the pancreatic enzyme is imporatnt as glucose sensor in insulin secretion and blood glucose homeostasis, interaction of ATP and glucose during binding to the enzyme ADP + D-glucose 6-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli to homogeneity Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Homo sapiens
-
pancreatic beta cell
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
Vmax of wild-type and mutant enzymes Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-glucose
-
Homo sapiens ADP + D-glucose 6-phosphate
-
?
ATP + D-glucose the pancreatic enzyme is imporatnt as glucose sensor in insulin secretion and blood glucose homeostasis, interaction of ATP and glucose during binding to the enzyme Homo sapiens ADP + D-glucose 6-phosphate
-
?

Subunits

Subunits Comment Organism
More molecuar structure modeling Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP as MgATP2-, binding site structure, ATP binding involves residues Asp78, Thr82, Gly227, Thr228, and S336 Homo sapiens