HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 2.7.1.29 - glycerone kinase
for references in articles please use BRENDA:EC2.7.1.29
Word Map on EC 2.7.1.29
- 2.7.1.29
- 1,3-propanediol
-
dissimilation
- freundii
-
citrobacter
-
dhal
- pt
-
hemiaminal
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
2.7.1.29
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
glycerone kinase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP:glycerone phosphotransferase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9027-47-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
?
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
?
-
-
no activity with glycerol, hydroxyacetone, hydroxypyruvic acid, chloro-3-hydroxyacetone, and methylglyoxal
-
-
-
additional information
?
-
the enzyme does not show activity with GTP, CTP, TTP and UTP, inorganic triphosphate, and polyphosphate
-
-
-
additional information
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62245
2 * 62245, recombinant enzyme, deduced from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
65
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.29)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
