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Literature summary for 2.7.1.1 extracted from

  • Fornaini, G.; Dacha, M.; Magnani, M.; Stocchi, V.
    Hexokinase from rabbit red blood cells (1982), Methods Enzymol., 90, 3-10.
No PubMed abstract available

General Stability

General Stability Organism
D-glucose or D-fructose, 5 mM, stabilizes Oryctolagus cuniculus
glycerol, 9-15% v/v, stabilizes Oryctolagus cuniculus
sulfhydryl protecting agents stabilize Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
ATP uncomplexed, competitive to MgATP2-, erythrocyte enzyme Oryctolagus cuniculus
D-glucose 6-phosphate linear competitive inhibition with MgATP2- as varied substrate Oryctolagus cuniculus
GSSG strong inhibitor at all concentrations Oryctolagus cuniculus
Mg2+ competitive to MgATP2-; uncomplexed Oryctolagus cuniculus
MgADP- erythrocyte enzyme, mixed inhibitor versus MgATP2- and D-glucose Oryctolagus cuniculus
N-acetyl-D-glucosamine competitive to glucose; erythrocyte enzyme; noncompetitive to MgATP2- Oryctolagus cuniculus
reduced glutathione 1 mM: reduced state of the enzyme with full catalytic activity, marked inhibition at high concentrations Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
D-glucose reticulocyte hexokinase Ia Oryctolagus cuniculus
0.06
-
D-glucose erythrocyte enzyme Oryctolagus cuniculus
0.125
-
D-glucose reticulocyte hexokinase Ib Oryctolagus cuniculus
0.5
-
ATP MgATP2- Oryctolagus cuniculus
0.5
-
ATP reticulocyte and erythrocyte enzymes Oryctolagus cuniculus
0.6
-
ATP MgATP2-, erythrocyte enzyme Oryctolagus cuniculus
0.71
-
D-mannose erythrocyte enzyme Oryctolagus cuniculus
1.33
-
2-deoxy-D-glucose erythrocyte enzyme Oryctolagus cuniculus
1.9
-
ITP MgITP2-, erythrocyte enzyme Oryctolagus cuniculus
2
-
D-glucosamine erythrocyte enzyme Oryctolagus cuniculus
17.8
-
D-fructose erythrocyte enzyme Oryctolagus cuniculus
41.6
-
N-acetyl-D-glucosamine erythrocyte enzyme Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
104000
-
1 * 104000, reticulocyte hexokinase Ia and Ib, SDS-PAGE Oryctolagus cuniculus
105000
-
reticulocyte hexokinase Ia and Ib, gel filtration, sucrose density gradient sedimentation Oryctolagus cuniculus
110000
-
gel filtration Oryctolagus cuniculus
110000
-
erythrocyte enzyme Oryctolagus cuniculus
112000
-
erythrocyte enzyme, sedimentation velocity Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
erythrocyte enzyme and reticulocyte hexokinase Ia and Ib Oryctolagus cuniculus
erythrocyte enzyme: 300000fold Oryctolagus cuniculus

Reaction

Reaction Comment Organism Reaction ID
ATP + D-hexose = ADP + D-hexose 6-phosphate rapid random kinetic mechanism, erythrocyte enzyme and hexokinase I Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte only one enzyme form Oryctolagus cuniculus
-
reticulocyte hexokinase Ia and Ib Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
144
-
reticulocyte, hexokinase Ib, at 37°C Oryctolagus cuniculus
145.6
-
erythrocyte, at 37°C Oryctolagus cuniculus
155
-
reticulocyte, hexokinase Ia, at 37°C Oryctolagus cuniculus

Storage Stability

Storage Stability Organism
-20°C, 5 mM sodium-potassium phosphate buffer, pH 7.5, erythrocyte enzyme is more stable than in other buffer systems Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2-deoxy-D-glucose 65.7% of the activity with glucose, erythrocyte enzyme Oryctolagus cuniculus ADP + 2-deoxy-D-glucose 6-phosphate
-
?
D-fructose + ATP 70% of the activity with glucose, erythrocyte enzyme Oryctolagus cuniculus ADP + D-fructose 6-phosphate
-
?
D-glucosamine + ATP erythrocyte enzyme, 43.4% of the activity with glucose Oryctolagus cuniculus ADP + D-glucosamine 6-phosphate
-
?
D-glucose + ATP MgATP2- Oryctolagus cuniculus ADP + D-glucose 6-phosphate
-
?
D-mannose + ATP 109% of the activity with glucose, erythrocyte enzyme Oryctolagus cuniculus ADP + D-mannose 6-phosphate
-
?
ITP + D-glucose 36% of the activity with ATP, erythrocyte enzyme Oryctolagus cuniculus IDP + D-glucose 6-phosphate
-
?
ITP + D-glucose MgITP Oryctolagus cuniculus IDP + D-glucose 6-phosphate
-
?
additional information not: D-galactose Oryctolagus cuniculus ?
-
?
N-acetyl-D-glucosamine + ATP erythrocyte enzyme, 32.6% of the activity with glucose Oryctolagus cuniculus ADP + N-acetyl-D-glucosamine 6-phosphate
-
?

Subunits

Subunits Comment Organism
monomer 1 * 110000, erythrocyte enzyme, SDS-PAGE Oryctolagus cuniculus
monomer 1 * 104000, reticulocyte hexokinase Ia and Ib, SDS-PAGE Oryctolagus cuniculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Oryctolagus cuniculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.025
-
D-glucose 6-phosphate
-
Oryctolagus cuniculus
0.7
-
N-acetyl-D-glucosamine erythrocyte enzyme, competitive to glucose Oryctolagus cuniculus
1.5
-
ATP uncomplexed ATP, erythrocyte enzyme, competitive to MgATP2- Oryctolagus cuniculus
3
-
MgADP- erythrocyte enzyme, mixed inhibitor versus MgATP2- Oryctolagus cuniculus
7.8
-
MgADP- erythrocyte enzyme, mixed inhibitor versus glucose Oryctolagus cuniculus
9
-
Mg2+ erythrocyte enzyme, uncomplexed Mg2+ Oryctolagus cuniculus

pI Value

Organism Comment pI Value Maximum pI Value
Oryctolagus cuniculus under native conditions
-
5.7
Oryctolagus cuniculus reticulocyte hexokinase Ib
-
5.7
Oryctolagus cuniculus erythrocyte enzyme and reticulocyte hexokinase Ia, under native conditions
-
6.2