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Information on EC 2.7.1.29 - glycerone kinase
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2.7.1.29 glycerone kinaseSpecify your search results
Word Map
- 2.7.1.29
- freundii
- 1,3-propanediol
-
dissimilation
- pt
-
dhal
-
phosphoenolpyruvate-dependent
-
hemiaminal
-
phosphoenolpyruvate:carbohydrate
- biofuel production
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
acetol kinase, dAK, DHA kinase, DhaK, DhaK-2, DhaKI, DhaL, dihydroxyacetone kinase, dihydroxyacetone kinase I, FMN cyclase/dha kinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetol kinase
-
-
-
-
dAK
DHA kinase
DhaK
DhaK-2
DhaKI
dihydroxyacetone kinase
dihydroxyacetone kinase I
FMN cyclase/dha kinase
glycerone kinase
-
-
-
-
kinase, acetol (phosphorylating)
-
-
-
-
additional information
DHA kinase
-
-
-
-
dihydroxyacetone kinase
-
-
-
-
additional information
-
dihydroxyacetoe phosphate kinases exist in 2 different groups, one utilizing ATP as phosphate donor, the other utilizing phosphoenolpyruvate
additional information
-
dihydroxyacetone phosphate kinases exist in 2 different groups, one utilizing ATP as phosphate donor, the other utilizing phosphoenolpyrivate
additional information
-
dihydroxyacetoe phosphate kinases exist in 2 different groups, one utilizing ATP as phosphate donor, the other utilizing phosphoenolpyrivate
additional information
-
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
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + glycerone = ADP + glycerone phosphate
-
-
-
-
ATP + glycerone = ADP + glycerone phosphate
covalent substrate-binding and random bi bi kinetic mechanism
-
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
-
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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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
ATP + acetol
ADP + acetol phosphate
-
i.e. 1-hydroxy-2-propanone
-
?
ATP + DL-glyceraldehyde
ADP + DL-glyceraldehyde 3-phosphate
-
D,L-glyceraldehyde binds strongly to the enzyme, slow product release
-
-
?
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
-
-
-
-
?
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
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
Q1KLC3
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
essential for methanol assimilation
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
involved in detoxification of dihydroxyacetone
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
?
ATP + DL-glyceraldehyde
ADP + glyceraldehyde 3-phosphate
-
25% of the activity with dihydroxyacetone
-
?
ATP + DL-glyceraldehyde
ADP + glyceraldehyde 3-phosphate
-
25% of the activity with dihydroxyacetone
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
i.e. dihydroxyacetone phosphate
-
?
CTP + dihydroxyacetone
CDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
CTP + dihydroxyacetone
CDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
CTP + dihydroxyacetone
CDP + dihydroxyacetone phosphate
-
lower than 1% of the activity with ATP
-
?
GTP + dihydroxyacetone
GDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
GTP + dihydroxyacetone
GDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
GTP + dihydroxyacetone
GDP + dihydroxyacetone phosphate
-
lower than 1% of the activity with ATP
-
?
ITP + dihydroxyacetone
IDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
ITP + dihydroxyacetone
IDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
ITP + dihydroxyacetone
IDP + dihydroxyacetone phosphate
-
11.2% of activity with ATP
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
-
-
i.e. dihydroxyacetone phosphate
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
-
i.e. dihydroxyacetone phosphate
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
regulation involving de-/phosphorylation, and the 3 subunits with ADP and transcription factor DhaR, overview
-
-
?
UTP + dihydroxyacetone
UDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
UTP + dihydroxyacetone
UDP + dihydroxyacetone phosphate
-
3.1% of the activity with ATP
-
?
additional information
?
-
enzyme is confirmed by total proteome analysis of glycerol-grown cells
-
-
-
additional information
?
-
-
no activity with glycerol, hydroxyacetone, hydroxypyruvic acid, chloro-3-hydroxyacetone, and methylglyoxal
-
-
-
additional information
?
-
Q1KLC3
the enzyme does not show activity with GTP, CTP, TTP and UTP, inorganic triphosphate, and polyphosphate
-
-
-
additional information
?
-
Q1KLC3
the enzyme does not show activity with GTP, CTP, TTP and UTP, inorganic triphosphate, and polyphosphate
-
-
-
additional information
?
-
-
the enzyme is involved in the pathway for glycerol oxidation
-
-
-
additional information
?
-
-
the enzyme is involved in the pathway for glycerol oxidation
-
-
-
additional information
?
-
-
no activity with glycerol, hydroxyacetone, hydroxypuruvic acid, chloro-3-hydroxyacetone, and methylglyoxal
-
-
-
additional information
?
-
-
the enzyme is part of a multicomponent enyzme 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
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
Q1KLC3
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
O74192
essential for methanol assimilation
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
P43550, P54838
involved in detoxification of dihydroxyacetone
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
i.e. dihydroxyacetone phosphate
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
-
-
i.e. dihydroxyacetone phosphate
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
P76015
regulation involving de-/phosphorylation, and the 3 subunits with ADP and transcription factor DhaR, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the pathway for glycerol oxidation
-
-
-
additional information
?
-
-
the enzyme is involved in the pathway for glycerol oxidation
-
-
-
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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
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Ca2+
-
can partially replace Mg2+ in activation, 30.3% of activity with Mg2+
Co2+
-
can partially replace Mg2+ in activation, 57.3% of activity with Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
both components of the MgATP complex inhibit the kinase at excess concentration
-
additional information
-
glycerol, hydroxyacetone, hydroxypuruvic acid, and methylglyoxal are no inhibitors
-
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hepatitis B, Chronic
Serum dihydroxyacetone kinase peptide m/z 520.3 as predictor of disease severity in patients with compensated chronic hepatitis B.
Melanoma
Mechanisms of immune evasion induced by a complex of dengue virus and preexisting enhancing antibodies.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00122
dihydroxyacetone
-
pH and temperature not specified in the publication
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; pH 7.5, 30°C, DhaK-DhaL-DhaM complex; 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
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; pH 7.5, 30°C, DhaK-DhaL-DhaM complex; 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
24.13
dihydroxyacetone
-
pH and temperature not specified in the publication
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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
19800
dihydroxyacetone
-
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
Show AA Sequence and Transmembrane Helices (1170 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62245
2 * 62245, recombinant enzyme, deduced from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
trimer
additional information
dimer
2 * 62000, recombinant enzyme, SDS-PAGE; 2 * 62245, recombinant enzyme, deduced from amino acid sequence
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
approx. 18000 Da, monomeric state is suggested; approx. 35000 Da, monomeric state is suggested; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; 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; approx. 35000 Da, monomeric state is suggested; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; 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; approx. 35000 Da, monomeric state is suggested; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystal structure of enzyme complex with an ATP analogue and dihydroxyacetone at 2.5 A resolution
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
-
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
65
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol, most effective stabilizer, EDTA and MgCl2 stabilize to a lesser extent, inactivated during ammonium sulfate precipitation
-
not affected by 2 M glycerol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, butyl-Toyopearl, UNO-Q6, recombinant enzyme
DEAE-cellulose, Superdex 75; DEAE-cellulose, Superdex 75; HighQ anion exchange, Superdex 200
polyethylene glycol 6000, polyethyleneimine, DEAE-Sepharose, Sepharose CL-6B
-
streptomycin sulfate, ammonium sulfate, Cibacron blue F3G-ASephadex g-200, DEAE cellulose, partially purified
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli NM522 cells
expressed in Escherichia coli strain BL21(DE3) and in chloroplasts from Nicotiana tabacum cultivar Xanthi
-
overexpression in Escherichia coli; overexpression in Escherichia coli; overexpression in Escherichia coli
phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
inactivation of the gene lin0370 causes 20fold-elevated expression level of the dhaK-2 gene
the enzyme has nearly no activity changes under continuous cultivation from 0.5 to 3.0 M NaCl but the activity increases significantly with further increased salinities and achieves the maximum under 4.5 M NaCl
-
inactivation of the gene lin0370 causes 20fold-elevated expression level of the dhaK-2 gene
-
inactivation of the gene lin0370 causes 20fold-elevated expression level of the dhaK-2 gene
-
inactivation of the gene lin0370 causes 20fold-elevated expression level of the dhaK-2 gene
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sellinger, O.Z.; Miller, O.N.
Phosphorylation of acetol by homogenates of rat liver
Fed. Proc.
16
245-246
1957
Rattus norvegicus
-
brenda
Bystrykh, L.V.; de Koning, W.; Harder, W.
Triokinase from Candida boidinii KD1
Methods Enzymol.
188
445-451
1990
Candida boidinii, Candida boidinii KD1
brenda
Hofmann, K.H.; Babel, W.
Glycerone kinase from Candida methylica
Methods Enzymol.
188
451-455
1990
Candida methylica, Ogataea angusta, Ogataea angusta CBS 4732
brenda
Luers, G.H.; Advani, R.; Wenzel, T.; Subramani, S.
The Pichia pastoris dihydroxyacetone kinase is a PTS1-containing, but cytosolic, protein that is essential for growth on methanol
Yeast
14
759-771
1998
Komagataella pastoris, Komagataella pastoris (O74192)
brenda
Itoh, N.; Tujibata, Y.; Liu, J.Q.
Cloning and overexpression in Escherichia coli of the gene encoding dihydroxyacetone kinase isoenzyme I from Schizosaccharomyces pombe, and its application to dihydroxyacetone phosphate production
Appl. Microbiol. Biotechnol.
51
193-200
1999
Schizosaccharomyces pombe (O13902), Schizosaccharomyces pombe
brenda
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.
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2001
Escherichia coli, Escherichia coli (P37349), Escherichia coli (P76014), Escherichia coli (P76015)
brenda
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, Escherichia coli (P37349), Escherichia coli (P76014), Escherichia coli (P76015)
brenda
Molin, M.; Norbeck, J.; Blomberg, A.
Dihydroxyacetone kinases in Saccharomyces cerevisiae are involved in detoxification of dihydroxyacetone
J. Biol. Chem.
278
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2003
Saccharomyces cerevisiae (P43550), Saccharomyces cerevisiae (P54838)
brenda
Siebold, C.; Arnold, I.; Garcia-Alles, L.F.; Baumann, U.; Erni, B.
Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha -helical barrel ATP-binding domain
J. Biol. Chem.
278
48236-48244
2003
Citrobacter freundii, Citrobacter freundii (P45510)
brenda
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, Escherichia coli (P37349)
brenda
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
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2005
Escherichia coli, Escherichia coli (P76015)
brenda
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
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280
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2005
Citrobacter freundii, Escherichia coli
brenda
Cabezas, A.; Costas, M.J.; Pinto, R.M.; Couto, A.; Cameselle, J.C.
Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases
Biochem. Biophys. Res. Commun.
338
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2005
Homo sapiens, Homo sapiens (Q3LXA3), Rattus norvegicus
brenda
Gonzalez-Pajuelo, M.; Meynial-Salles, I.; Mendes, F.; Soucaille, P.; Vasconcelos, I.
Microbial conversion of glycerol to 1,3-propanediol: physiological comparison of a natural producer, Clostridium butyricum VPI 3266, and an engineered strain, Clostridium acetobutylicum DG1(pSPD5)
Appl. Environ. Microbiol.
72
96-101
2006
Clostridium butyricum, Clostridium butyricum VPI 3266, no activity in Clostridium acetobutylicum, no activity in Clostridium acetobutylicum DG1(pSPD5)
brenda
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
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2006
Escherichia coli, Escherichia coli (Q0TIH0)
brenda
Iturrate, L.; Sanchez-Moreno, I.; Oroz-Guinea, I.; Perez-Gil, J.; Garcia-Junceda, E.
Preparation and characterization of a bifunctional aldolase/kinase enzyme: a more efficient biocatalyst for C-C bond formation
Chemistry
16
4018-4030
2010
Citrobacter freundii, Citrobacter freundii CECT 4626
brenda
Xiao, S.; Sun, Z.; Wang, S.; Zhang, J.; Li, K.; Chen, L.
Overexpressions of dihydroxyacetone synthase and dihydroxyacetone kinase in chloroplasts install a novel photosynthetic HCHO-assimilation pathway in transgenic tobacco using modified Gateway entry vectors
Acta Physiol. Plant.
34
1975-1985
2012
Komagataella pastoris, Komagataella pastoris GS115
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brenda
Monniot, C.; Zebre, A.C.; Ake, F.M.; Deutscher, J.; Milohanic, E.
Novel listerial glycerol dehydrogenase- and phosphoenolpyruvate-dependent dihydroxyacetone kinase system connected to the pentose phosphate pathway
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4972-4982
2012
Listeria innocua, Listeria innocua CLIP 11262, Listeria monocytogenes
brenda
Sauvageot, N.; Ladjouzi, R.; Benachour, A.; Rince, A.; Deutscher, J.; Hartke, A.
Aerobic glycerol dissimilation via the Enterococcus faecalis DhaK pathway depends on NADH oxidase and a phosphotransfer reaction from PEP to DhaK via EIIADha
Microbiology
158
2661-2666
2012
Enterococcus faecalis, Enterococcus faecalis JH2-2
brenda
Chen, H.; Lu, Y.; Jiang, J.G.
Comparative analysis on the key enzymes of the glycerol cycle metabolic pathway in Dunaliella salina under osmotic stresses
PLoS ONE
7
e37578
2012
Dunaliella salina
brenda
Shi, R.; McDonald, L.; Cui, Q.; Matte, A.; Cygler, M.; Ekiel, I.
Structural and mechanistic insight into covalent substrate binding by Escherichia coli dihydroxyacetone kinase
Proc. Natl. Acad. Sci. USA
108
1302-1307
2011
Escherichia coli, Escherichia coli (P76015)
brenda
Tan, H.; Xiao, S.; Han, S.; Xuan, X.; Sun, Z.; Li, K.; Chen, L.
The function of an installed photosynthetic formaldehyde-assimilation pathway containing dihydroxyacetone synthase and dihydroxyacetone kinase enhanced formaldehyde removal from solution in transgenic geranium leaves
Int. Biodeter. Biodegrad.
106
127-132
2016
Pelargonium sp.
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brenda
Sanchez-Moreno, I.; Bordes, I.; Castillo, R.; Ruiz-Pernia, J.J.; Moliner, V.; Garcia-Junceda, E.
Tuning the phosphoryl donor specificity of dihydroxyacetone kinase from ATP to inorganic polyphosphate. An insight from computational studies
Int. J. Mol. Sci.
16
27835-27849
2015
Citrobacter freundii, Citrobacter freundii (Q1KLC3), Citrobacter freundii CECT 4626 (Q1KLC3)
brenda
Wei, D.; Wang, M.; Jiang, B.; Shi, J.; Hao, J.
Role of dihydroxyacetone kinases I and II in the dha regulon of Klebsiella pneumoniae
J. Biotechnol.
177
13-19
2014
Klebsiella pneumoniae (A0A023T745), Klebsiella pneumoniae, Klebsiella pneumoniae CGMCC 1.6366 (A0A023T745)
brenda
Patil, Y.; Junghare, M.; Müller, N.
Fermentation of glycerol by Anaerobium acetethylicum and its potential use in biofuel production
Microb. Biotechnol.
10
203-217
2017
Anaerobium acetethylicum (A0A1D3TV19)
brenda
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