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Information on EC 2.7.1.29 - glycerone kinase and Organism(s) Escherichia coli and UniProt Accession P37349
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2.7.1.29 glycerone kinaseSpecify your search results
Word Map
- 2.7.1.29
-
dissimilation
- 1,3-propanediol
- freundii
- dhaklm
-
phosphoenolpyruvate-dependent
-
hemiaminal
-
phosphoenolpyruvate:carbohydrate
- biofuel production
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dihydroxyacetone kinase, dha kinase, phosphoenolpyruvate carbohydrate phosphotransferase, atp-dependent dihydroxyacetone kinase, pep-dependent dha kinase, dihydroxyacetone kinase i, dhaki, dhak-2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetol kinase
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DHA kinase
dihydroxyacetone kinase
glycerone kinase
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-
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kinase, acetol (phosphorylating)
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-
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additional information
DHA kinase
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-
-
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dihydroxyacetone kinase
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-
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-
additional information
dihydroxyacetoe phosphate kinases exist in 2 different groups, one utilizing ATP as phosphate donor, the other utilizing phosphoenolpyrivate
additional information
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dihydroxyacetoe phosphate kinases exist in 2 different groups, one utilizing ATP as phosphate donor, the other utilizing phosphoenolpyruvate
additional information
dihydroxyacetoe phosphate kinases exist in 2 different groups, one utilizing ATP as phosphate donor, the other utilizing phosphoenolpyrivate
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
ATP + glycerone = ADP + glycerone phosphate
nucleotide binding structure, mechanism, and function, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
ATP:glycerone phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
9027-47-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phospho-DhaM + 3,4-dihydroxy-2-butanone
dephospho-DhaM + 3-hydroxy-2-butanone-4-phosphate
-
-
?
phospho-DhaM + erythrose
dephospho-DhaM + erythrose 4-phosphate
-
-
?
phospho-DhaM + glyceraldehyde
dephospho-DhaM + glyceraldehyde 2-phosphate
-
-
?
phosphoenolpyruvate + DL-glyceraldehyde
pyruvate + DL-glyceraldehyde 3-phosphate
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-
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
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i.e. dihydroxyacetone phosphate
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?
phosphorylated DhaM domain of dihydroxyacetone kinase + dihydroxyacetone
dephospho-DhaM + dihydroxyacetone phosphate
enzyme complex uses the PEP:sugar phosphotransferase protein DhaM instead of ATP as phosphoryl donor
-
?
phospho-DhaM + 3,4-dihydroxy-2-butanone
dephospho-DhaM + 3-hydroxy-2-butanone-4-phosphate
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-
?
phospho-DhaM + erythrose
dephospho-DhaM + erythrose 4-phosphate
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-
?
phospho-DhaM + glyceraldehyde
dephospho-DhaM + glyceraldehyde 2-phosphate
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-
?
phosphorylated DhaM domain of dihydroxyacetone kinase + dihydroxyacetone
dephospho-DhaM + dihydroxyacetone phosphate
enzyme complex uses the PEP:sugar phosphotransferase protein DhaM instead of ATP as phosphoryl donor
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?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
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-
i.e. dihydroxyacetone phosphate
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?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
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i.e. dihydroxyacetone phosphate
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?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
regulation involving de-/phosphorylation, and the 3 subunits with ADP and transcription factor DhaR, overview
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-
?
additional information
?
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no activity with glycerol, hydroxyacetone, hydroxypuruvic acid, chloro-3-hydroxyacetone, and methylglyoxal
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-
?
additional information
?
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no activity with glycerol, hydroxyacetone, hydroxypuruvic acid, chloro-3-hydroxyacetone, and methylglyoxal
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-
?
additional information
?
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the enzyme is part of a multicomponent enzyme system, the phosphoenolpyruvate:sugar phosphotransferase system PTS
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
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-
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
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-
i.e. dihydroxyacetone phosphate
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
regulation involving de-/phosphorylation, and the 3 subunits with ADP and transcription factor DhaR, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition by glycerol, hydroxyacetone, hydroxypuruvic acid, and methylglyoxal
-
additional information
-
no inhibition by glycerol, hydroxyacetone, hydroxypuruvic acid, and methylglyoxal
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the DhaR transcription factor stimulates the transcription of the dhaKLM operon from a sigma70 promotor and autorepresses expression of DhaR
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additional information
-
the DhaR transcription factor stimulates the transcription of the dhaKLM operon from a sigma70 promotor and autorepresses expression of DhaR
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045
dihydroxyacetone
pH 7.5, 30°C, DhaK-DhaL-DhaM complex
0.008
dihydroxyacetone
apparent value, Km above 0.008 mM, wild type enzyme, in 50 mM potassium phosphate pH 7.5, at 22°C
0.045
dihydroxyacetone
pH 7.5, 30°C, DhaK-DhaL-DhaM complex
0.302
dihydroxyacetone
apparent value, mutant enzyme H56A, in 50 mM potassium phosphate pH 7.5, at 22°C
2.2
dihydroxyacetone
apparent value, mutant enzyme H56N, in 50 mM potassium phosphate pH 7.5, at 22°C
additional information
additional information
substrate binding constants and reaction kinetics, overview
-
additional information
additional information
-
substrate binding constants and reaction kinetics, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.8
dihydroxyacetone
pH 7.5, 30°C, DhaK-DhaL-DhaM complex
1.6
dihydroxyacetone
apparent value, mutant enzyme H56A, in 50 mM potassium phosphate pH 7.5, at 22°C
2.8
dihydroxyacetone
pH 7.5, 30°C, DhaK-DhaL-DhaM complex
3.72
dihydroxyacetone
apparent value, mutant enzyme H56N, in 50 mM potassium phosphate pH 7.5, at 22°C
8.45
dihydroxyacetone
apparent value, Km above 0.008 mM, wild type enzyme, in 50 mM potassium phosphate pH 7.5, at 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
dihydroxyacetone
apparent value, mutant enzyme H56N, in 50 mM potassium phosphate pH 7.5, at 22°C
5.3
dihydroxyacetone
apparent value, mutant enzyme H56A, in 50 mM potassium phosphate pH 7.5, at 22°C
954
dihydroxyacetone
apparent value, Km above 0.008 mM, wild type enzyme, in 50 mM potassium phosphate pH 7.5, at 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
enzyme exists of a small, a large, and a substrate binding subunit
trimer
additional information
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
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
additional information
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
-
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
approx. 18000 Da, monomeric state is suggested
additional information
approx. 18000 Da, monomeric state is suggested
additional information
approx. 18000 Da, monomeric state is suggested
additional information
approx. 35000 Da, monomeric state is suggested
additional information
approx. 35000 Da, monomeric state is suggested
additional information
approx. 35000 Da, monomeric state is suggested
additional information
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
-
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
DhaK and DhaK-dihydroxacetone complex are crystallized from 80 mM sodium acetate, pH 5.0, 160 mM ammonium sulfate, 17% polyethylene glycol 4000, 15% 2-methyl-2,4-pentanediol using hanging drop vapor diffusion, crystals diffract to 1.75 A resolution
DhaK-DhaL complex bound to ADP anddihydroxyacetone, hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 3.5 M sodium formate or 0.1 M sodium citrate pH 5.6, 20% (w/v)PEG 8000, at 19°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H56A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
H56N
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel affinity column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gutknecht, R.; Beutler, R.; Garcia-Alles, L.F.; Baumann, U.; Erni, B.
The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor
EMBO J.
20
2480-2486
2001
Escherichia coli (P37349), Escherichia coli (P76014), Escherichia coli (P76015), Escherichia coli
Siebold, C.; Garcia-Alles, L.F.; Erni, B.; Baumann, U.
A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase
Proc. Natl. Acad. Sci. USA
100
8188-8192
2003
Escherichia coli (P37349), Escherichia coli (P76014), Escherichia coli (P76015), Escherichia coli
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
Biochemistry
43
13037-13045
2004
Citrobacter freundii, Escherichia coli (P37349), Escherichia coli
Bachler, C.; Schneider, P.; Bahler, P.; Lustig, A.; Erni, B.
Escherichia coli dihydroxyacetone kinase controls gene expression by binding to transcription factor DhaR
EMBO J.
24
283-293
2005
Escherichia coli (P76015), Escherichia coli
Bachler, C.; Flukiger-Bruhwiler, K.; Schneider, P.; Bahler, P.; Erni, B.
From ATP as substrate to ADP as coenzyme: functional evolution of the nucleotide binding subunit of dihydroxyacetone kinases
J. Biol. Chem.
280
18321-18325
2005
Citrobacter freundii, Escherichia coli
Oberholzer, A.E.; Schneider, P.; Baumann, U.; Erni, B.
Crystal structure of the nucleotide-binding subunit DhaL of the Escherichia coli dihydroxyacetone kinase
J. Mol. Biol.
359
539-545
2006
Escherichia coli (P76014), Escherichia coli
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