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Literature summary for 2.7.1.29 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)

Crystallization (Comment) Organism
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

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Citrobacter freundii

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Citrobacter freundii
-
-
-
Escherichia coli P37349
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + glycerone = ADP + glycerone phosphate covalent substrate-binding and random bi bi kinetic mechanism Citrobacter freundii
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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Citrobacter freundii

Ki Value [mM]

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