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Literature summary extracted from

  • Garcia-Alles, L.F.; Siebold, C.; Nyffeler, T.L.; Flukiger-Bruhwiler, K.; Schneider, P.; Burgi, H.B.; Baumann, U.; Erni, B.
    Phosphoenolpyruvate- and ATP-dependent dihydroxyacetone kinases: covalent substrate-binding and kinetic mechanism (2004), Biochemistry, 43, 13037-13045.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.29 apoenzyme, from solution containing 80 mM sodium acetate, pH 5.0, 160 mM ammonium sulfate, 17% w/v PEG 4000, 15% w/v methylpentanediol, hanging drop vapour diffusion method, apoenzyme-crystals are soaked in 2 mM glyceraldehyde or 5 mM dihydroxyacetone phosphate and flash frozen at -168°C, X-ray diffraction structure determination and analysis at 2.0 and 1.9 A resolution, respectively Escherichia coli

General Stability

EC Number General Stability Organism
2.7.1.29 enzyme-D,L-glyceraldehyde complex is resistant to SDS Citrobacter freundii
2.7.1.29 not affected by 2 M glycerol Citrobacter freundii
2.7.1.29 not affected by 2 M glycerol Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.29 ADP competitive to ATP, noncompetitive to D,L-glyceraldehyde Citrobacter freundii
2.7.1.29 chloro-3-hydroxyacetone binds to the active site Citrobacter freundii
2.7.1.29 chloro-3-hydroxyacetone binds to the active site Escherichia coli
2.7.1.29 D,L-glyceraldehyde competitive Citrobacter freundii
2.7.1.29 D,L-glyceraldehyde competitive Escherichia coli
2.7.1.29 additional information glycerol, hydroxyacetone, hydroxypuruvic acid, and methylglyoxal are no inhibitors Citrobacter freundii
2.7.1.29 additional information no inhibition by glycerol, hydroxyacetone, hydroxypuruvic acid, and methylglyoxal Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.29 additional information
-
 additional information substrate binding constants and reaction kinetics, overview Citrobacter freundii
2.7.1.29 additional information
-
 additional information substrate binding constants and reaction kinetics, overview Escherichia coli
2.7.1.29 0.005
-
 glycerone phosphate or below, pH 7.5, 30°C Citrobacter freundii
2.7.1.29 0.006
-
 glycerone phosphate pH 7.5, 30°C Escherichia coli
2.7.1.29 0.1
-
 ATP pH 7.5, 30°C Citrobacter freundii
2.7.1.29 0.18
-
 D,L-glyceraldehyde pH 7.5, 30°C Citrobacter freundii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.29 Mg2+
-
 Citrobacter freundii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.29 ATP + glycerone Citrobacter freundii
-
 ADP + glycerone phosphate
-
 ?
2.7.1.29 phosphoenolpyruvate + glycerone Escherichia coli
-
 pyruvate + glycerone phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.29 Citrobacter freundii
-
-
-
2.7.1.29 Escherichia coli P37349
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.29 ATP + glycerone = ADP + glycerone phosphate covalent substrate-binding and random bi bi kinetic mechanism Citrobacter freundii
a
2.7.1.29 ATP + glycerone = ADP + glycerone phosphate substrates and products are bound in hemiaminal linkage to the active site histidine, thereby not activating the cataltically reacting hydroxyl group Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.29 ATP + DL-glyceraldehyde D,L-glyceraldehyde binds strongly to the enzyme, slow product release Citrobacter freundii ADP + DL-glyceraldehyde 3-phosphate
-
 ?
2.7.1.29 ATP + glycerone
-
 Citrobacter freundii ADP + glycerone phosphate
-
 ?
2.7.1.29 ATP + glycerone
-
 Citrobacter freundii ADP + glycerone phosphate i.e. dihydroxyacetone phosphate ?
2.7.1.29 additional information no activity with glycerol, hydroxyacetone, hydroxypuruvic acid, chloro-3-hydroxyacetone, and methylglyoxal Escherichia coli ?
-
 ?
2.7.1.29 additional information no activity with glycerol, hydroxyacetone, hydroxypyruvic acid, chloro-3-hydroxyacetone, and methylglyoxal Citrobacter freundii ?
-
 ?
2.7.1.29 phosphoenolpyruvate + DL-glyceraldehyde
-
 Escherichia coli pyruvate + DL-glyceraldehyde 3-phosphate
-
 ?
2.7.1.29 phosphoenolpyruvate + glycerone
-
 Escherichia coli pyruvate + glycerone phosphate
-
 ?
2.7.1.29 phosphoenolpyruvate + glycerone
-
 Escherichia coli pyruvate + glycerone phosphate i.e. dihydroxyacetone phosphate ?

Subunits

EC Number Subunits Comment Organism
2.7.1.29 trimer enzyme exists of a small, a large, and a substrate binding subunit Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.1.29 DHA kinase
-
 Citrobacter freundii
2.7.1.29 DHA kinase
-
 Escherichia coli
2.7.1.29 DhaK
-
 Citrobacter freundii
2.7.1.29 DhaK
-
 Escherichia coli
2.7.1.29 dihydroxyacetone kinase
-
 Citrobacter freundii
2.7.1.29 dihydroxyacetone kinase
-
 Escherichia coli
2.7.1.29 More dihydroxyacetoe phosphate kinases exist in 2 different groups, one utilizing ATP as phosphate donor, the other utilizing phosphoenolpyrivate Escherichia coli
2.7.1.29 More dihydroxyacetone phosphate kinases exist in 2 different groups, one utilizing ATP as phosphate donor, the other utilizing phosphoenolpyrivate Citrobacter freundii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.29 30
-
 phosphotransferase assay at Citrobacter freundii
2.7.1.29 30
-
 phosphotransferase assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.29 4.8
-
 glycerone phosphate pH 7.5, 30°C Escherichia coli
2.7.1.29 5.17
-
 D,L-glyceraldehyde pH 7.5, 30°C Citrobacter freundii
2.7.1.29 17.5
-
 glycerone phosphate pH 7.5, 30°C Citrobacter freundii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.29 7.5
-
 phosphotransferase assay at Citrobacter freundii
2.7.1.29 7.5
-
 phosphotransferase assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.29 ATP dependent on Citrobacter freundii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.1.29 additional information
-
 additional information inhibition kinetics Citrobacter freundii
2.7.1.29 additional information
-
 additional information inhibition kinetics Escherichia coli
2.7.1.29 0.14
-
 ADP pH 7.5, 30°C Citrobacter freundii
2.7.1.29 0.15
-
 D,L-glyceraldehyde pH 7.5, 30°C Escherichia coli
2.7.1.29 0.6
-
 D,L-glyceraldehyde pH 7.5, 30°C Citrobacter freundii