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Literature summary for 2.7.1.29 extracted from
- From ATP as substrate to ADP as coenzyme: functional evolution of the nucleotide binding subunit of dihydroxyacetone kinases (2005), J. Biol. Chem., 280, 18321-18325.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| phylogenetic analysis | Escherichia coli |
| phylogenetic analysis | Citrobacter freundii |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | - |
Escherichia coli |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + glycerone | Citrobacter freundii | - |
ADP + glycerone phosphate | i.e. dihydroxyacetone phosphate | ? | |
| phosphoenolpyruvate + glycerone | Escherichia coli | - |
pyruvate + glycerone phosphate | i.e. dihydroxyacetone phosphate | ? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Citrobacter freundii | - |
- |
- |
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + glycerone = ADP + glycerone phosphate | nucleotide binding structure, mechanism, and function, overview | Escherichia coli | |
| ATP + glycerone = ADP + glycerone phosphate | nucleotide binding structure, mechanism, and function, overview | Citrobacter freundii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + glycerone | - |
Citrobacter freundii | ADP + glycerone phosphate | i.e. dihydroxyacetone phosphate | ? | |
| additional information | the enzyme is part of a multicomponent enzyme system, the phosphoenolpyruvate:sugar phosphotransferase system PTS | Escherichia coli | ? | - |
? | |
| phosphoenolpyruvate + glycerone | - |
Escherichia coli | pyruvate + glycerone phosphate | i.e. dihydroxyacetone phosphate | ? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| trimer | enzyme exists of 3 subunit DhaK, DhaM, and DhaL: DhaK contains the dihydroxyacetone phosphate binding site, DhaL contains ADP as cofactor for phosphate double displacement from DhaM to dihydroxyacetone phosphate, and DhaM provides a phospho-histidine relay between phosphoenolpyruvate and DhaL-ADP | Escherichia coli |
| trimer | enzyme exists of 3 subunit DhaK, DhaM, and DhaL: DhaK contains the dihydroxyacetone phosphate binding site, DhaL contains ADP as cofactor for phosphate double displacement from DhaM to dihydroxyacetone phosphate, and DhaM provides a phospho-histidine relay between phosphoenolpyruvate and DhaL-ADP | Citrobacter freundii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dihydroxyacetone kinase | - |
Escherichia coli |
| dihydroxyacetone kinase | - |
Citrobacter freundii |
| More | dihydroxyacetoe phosphate kinases exist in 2 different groups, one utilizing ATP as phosphate donor, the other utilizing phosphoenolpyruvate | Escherichia coli |
| More | dihydroxyacetoe phosphate kinases exist in 2 different groups, one utilizing ATP as phosphate donor, the other utilizing phosphoenolpyruvate | Citrobacter freundii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
| 37 | - |
assay at | Citrobacter freundii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
unfolding temperature for the apo-enzyme | Escherichia coli |
| 40 | - |
unfolding temperature for the apo-enzyme | Citrobacter freundii |
| 65 | - |
unfolding temperature for the ADP-bound enzyme | Escherichia coli |
| 65 | - |
unfolding temperature for the ADP-bound enzyme | Citrobacter freundii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Escherichia coli |
| 7.5 | - |
assay at | Citrobacter freundii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ADP | subunit DhaL contains ADP as cofactor for phosphate double displacement from subunit DhaM to dihydroxyacetone phosphate, evolution of the binding site, conversion of a substrate binding site into a cofactor binding site, overview, complexing with the enzyme increases the thermal unfolding temperature | Escherichia coli | |
| ADP | subunit DhaL contains ADP as cofactor for phosphate double displacement from subunit DhaM to dihydroxyacetone phosphate, evolution of the binding site, conversion of a substrate binding site into a cofactor binding site, overview, complexing with the enzyme increases the thermal unfolding temperature | Citrobacter freundii | |
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