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Literature summary for 2.7.1.29 extracted from

  • Bachler, C.; Schneider, P.; Bahler, P.; Lustig, A.; Erni, B.
    Escherichia coli dihydroxyacetone kinase controls gene expression by binding to transcription factor DhaR (2005), EMBO J., 24, 283-293.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information the DhaR transcription factor stimulates the transcription of the dhaKLM operon from a sigma70 promotor and autorepresses expression of DhaR Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphoenolpyruvate + glycerone Escherichia coli regulation involving de-/phosphorylation, and the 3 subunits with ADP and transcription factor DhaR, overview pyruvate + glycerone phosphate
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli P76015 subunit DhaK
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + glycerone
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Escherichia coli pyruvate + glycerone phosphate i.e. dihydroxyacetone phosphate ?
phosphoenolpyruvate + glycerone regulation involving de-/phosphorylation, and the 3 subunits with ADP and transcription factor DhaR, overview Escherichia coli pyruvate + glycerone 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

Synonyms

Synonyms Comment Organism
DHA kinase
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Escherichia coli
dihydroxyacetone kinase
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Escherichia coli
More dihydroxyacetoe phosphate kinases exist in 2 different groups, one utilizing ATP as phosphate donor, the other utilizing phosphoenolpyrivate Escherichia coli
phosphoenolpyruvate carbohydrate phosphotransferase
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Escherichia coli