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Literature summary for 2.7.1.1 extracted from
- A hexokinase with broad sugar specificity from a thermophilic bacterium (2005), Biochem. Biophys. Res. Commun., 334, 754-763.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| subcloning and expression in Escherichia coli strains DH5 alpha and MV1184 | Thermus caldophilus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | slight inhibition | Thermus caldophilus |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | 79% of the activity with Mg2+ | Thermus caldophilus | |
| Mg2+ | divalent metal ions are essential for activity, most effective metal ion, construction of a model of the enzyme-ATP/Mg2+-sugar-binding complex structure | Thermus caldophilus | |
| Mn2+ | 73% of the activity with Mg2+ | Thermus caldophilus | |
| additional information | different buffers have no effect on the enzyme activity | Thermus caldophilus | |
| Ni2+ | 92% of the activity with Mg2+ | Thermus caldophilus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 31000 | - |
4 * 31000, recombinant enzyme, SDS-PAGE, 4 * 31426, sequence calculation | Thermus caldophilus |
| 31426 | - |
4 * 31000, recombinant enzyme, SDS-PAGE, 4 * 31426, sequence calculation | Thermus caldophilus |
| 120000 | - |
recombinant enzyme, gel filtration | Thermus caldophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus caldophilus | Q5RLG0 | - |
- |
| Thermus caldophilus GK24 | Q5RLG0 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli strain MV1184, to homogeneity by heat precipitation at 80°C, successive ion exchange chromatography and gel filtration | Thermus caldophilus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + D-hexose = ADP + D-hexose 6-phosphate | substrate binding mechanism and structure | Thermus caldophilus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 196 | - |
purified recombinant enzyme | Thermus caldophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 2-deoxy-D-glucose | 42% of the activity with D-glucose | Thermus caldophilus | ADP + 2-deoxy-D-glucose 6-phosphate | - |
? | |
| ATP + 2-deoxy-D-glucose | 42% of the activity with D-glucose | Thermus caldophilus GK24 | ADP + 2-deoxy-D-glucose 6-phosphate | - |
? | |
| ATP + D-allose | 58% of the activity with D-glucose | Thermus caldophilus | ADP + D-allose 6-phosphate | - |
? | |
| ATP + D-allose | 58% of the activity with D-glucose | Thermus caldophilus GK24 | ADP + D-allose 6-phosphate | - |
? | |
| ATP + D-fructose | 16% of the activity with D-glucose | Thermus caldophilus | ADP + D-fructose 6-phosphate | - |
? | |
| ATP + D-glucosamine | 67% of the activity with D-glucose | Thermus caldophilus | ADP + D-glucosamine 6-phosphate | - |
? | |
| ATP + D-glucosamine | 67% of the activity with D-glucose | Thermus caldophilus GK24 | ADP + D-glucosamine 6-phosphate | - |
? | |
| ATP + D-glucose | best substrate | Thermus caldophilus | ADP + D-glucose 6-phosphate | - |
? | |
| ATP + D-glucose | best substrate | Thermus caldophilus GK24 | ADP + D-glucose 6-phosphate | - |
? | |
| ATP + D-mannose | 75% of the activity with D-glucose | Thermus caldophilus | ADP + D-mannose 6-phosphate | - |
? | |
| additional information | no activity with D-galactose and N-acetylglucosamine, enzyme shows broad substrate specificity, specificity probably depends on the interaction energy occurring by the positional proximity of sugars bound in the active site | Thermus caldophilus | ? | - |
? | |
| additional information | no activity with D-galactose and N-acetylglucosamine, enzyme shows broad substrate specificity, specificity probably depends on the interaction energy occurring by the positional proximity of sugars bound in the active site | Thermus caldophilus GK24 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme-ATP/Mg2+-sugar-binding complex structure modeling | Thermus caldophilus |
| tetramer | 4 * 31000, recombinant enzyme, SDS-PAGE, 4 * 31426, sequence calculation | Thermus caldophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | ROK-type, i.e. repressor kinase | Thermus caldophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | 80 | - |
Thermus caldophilus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 90 | weak activity at 30°C, high activity at 90°C, rapid decrease in activity above 90°C | Thermus caldophilus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
active up to 240 min | Thermus caldophilus |
| 90 | - |
loss of 90% activity within 60 min, complete inactivation within 120 min | Thermus caldophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Thermus caldophilus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 11 | low activities at pH 4.0 and pH 11.0 | Thermus caldophilus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | construction of a model of the enzyme-ATP/Mg2+-sugar-binding complex structure | Thermus caldophilus | |
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