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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
-
dissimilation
- 1,3-propanediol
- freundii
- dhaklm
-
phosphoenolpyruvate-dependent
-
hemiaminal
-
phosphoenolpyruvate:carbohydrate
- biofuel production
The enzyme appears in viruses and cellular organisms
Synonyms
dihydroxyacetone kinase, dha kinase, phosphoenolpyruvate carbohydrate phosphotransferase, atp-dependent dihydroxyacetone kinase, dhaki, pep-dependent dha kinase, dihydroxyacetone kinase i, dhak-2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetol kinase
-
-
-
-
ATP-dependent dihydroxyacetone kinase
dAK
DHA kinase
DhaK
DhaK-2
DhaKI
DhaL
dihydroxyacetone kinase
dihydroxyacetone kinase I
FMN cyclase/dha kinase
glycerone kinase
-
-
-
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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 phosphoenolpyruvate
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 phosphoenolpyrivate
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + glycerone = ADP + glycerone phosphate
-
-
-
-
ATP + glycerone = ADP + glycerone phosphate
Citrobacter freundii
-
-
-
ATP + glycerone = ADP + glycerone phosphate
Escherichia coli
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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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
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
-
-
?
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 + 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
-
-
-
ir
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 + 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
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
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
-
-
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
-
-
i.e. dihydroxyacetone phosphate
-
?
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
?
-
the enzyme does not show activity with GTP, CTP, TTP and UTP, inorganic triphosphate, and polyphosphate
-
-
?
additional information
?
-
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the enzyme does not show activity with GTP, CTP, TTP and UTP, inorganic triphosphate, and polyphosphate
-
-
?
additional information
?
-
Citrobacter freundii CECT 4626
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
?
-
Clostridium butyricum VPI 3266
-
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
?
-
-
no activity with glycerol, hydroxyacetone, hydroxypuruvic acid, chloro-3-hydroxyacetone, and methylglyoxal
-
-
?
additional information
?
-
-
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
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
essential for methanol assimilation
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
involved in detoxification of dihydroxyacetone
-
?
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 + glycerone
ADP + glycerone phosphate
-
-
i.e. dihydroxyacetone phosphate
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone 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
-
-
?
additional information
?
-
-
the enzyme is involved in the pathway for glycerol oxidation
-
-
?
additional information
?
-
Clostridium butyricum VPI 3266
-
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+
Mg2+
required, the phosphate groups of the nucleotide are coordinated via two magnesium ions to the side-chain carboxyl groups of aspartates
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
glycerol, hydroxyacetone, hydroxypuruvic acid, and methylglyoxal are no inhibitors
-
additional information
no inhibition by glycerol, hydroxyacetone, hydroxypuruvic acid, and methylglyoxal
-
additional information
-
no inhibition by glycerol, hydroxyacetone, hydroxypuruvic acid, and methylglyoxal
-
additional information
-
both components of the MgATP complex inhibit the kinase at excess concentration
-
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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
-
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
DAK inhibits MDA5-mediated signaling in the antiviral innate immunity of black carp.
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
0.045
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
0.302
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
0.00122
dihydroxyacetone
-
pH and temperature not specified in the publication
additional information
additional information
-
substrate binding constants and reaction kinetics, overview
-
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
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
19800
dihydroxyacetone
-
pH and temperature not specified in the publication
954
dihydroxyacetone
apparent value, Km above 0.008 mM, wild type enzyme, in 50 mM potassium phosphate pH 7.5, at 22°C
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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
Citrobacter freundii CECT 4626
dihydroxyacetone kinase subunits DhaK and DhaL
UniProt
brenda
dihydroxyacetone kinase subunits DhaK and DhaL
UniProt
brenda
dihydroxyacetone kinase subunits DhaK and DhaL
UniProt
brenda
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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
evolution
additional information
evolution
analysis of the glycerol metabolism genes in metagenomes suggests that Halorubrum and Haloquadratum possess mostly dihydroxyacetone kinase genes while Salinibacter possesses mostly glycerol-3-phosphate dehydrogenase genes. Family abundance of genes dhaL and dhaK, phylogenetic analysis. Across gene family, taxonomic affiliations of the dihydroxyacetone kinase families are closest to each other, as well as those of the alcohol dehydrogenase (Fe-ADH) and glycerol kinase (FGGY) gene families. Haloquadratum associates with dihydroxyacetone kinase gene families in the SS19, SS33, and SS37 metagenomes. By using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
evolution
B9LNV8; B9LNV9
analysis of the glycerol metabolism genes in metagenomes suggests that Halorubrum and Haloquadratum possess mostly dihydroxyacetone kinase genes while Salinibacter possesses mostly glycerol-3-phosphate dehydrogenase genes. Family abundance of genes dhaL and dhaK, phylogenetic analysis. Across gene family, taxonomic affiliations of the dihydroxyacetone kinase families are closest to each other, as well as those of the alcohol dehydrogenase (Fe-ADH) and glycerol kinase (FGGY) gene families. Halorubrum associates with dihydroxyacetone kinase gene families in the IC21 and Cahuil metagenomes. By using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
evolution
-
analysis of the glycerol metabolism genes in metagenomes suggests that Halorubrum and Haloquadratum possess mostly dihydroxyacetone kinase genes while Salinibacter possesses mostly glycerol-3-phosphate dehydrogenase genes. Family abundance of genes dhaL and dhaK, phylogenetic analysis. Across gene family, taxonomic affiliations of the dihydroxyacetone kinase families are closest to each other, as well as those of the alcohol dehydrogenase (Fe-ADH) and glycerol kinase (FGGY) gene families. Haloquadratum associates with dihydroxyacetone kinase gene families in the SS19, SS33, and SS37 metagenomes. By using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
-
evolution
-
analysis of the glycerol metabolism genes in metagenomes suggests that Halorubrum and Haloquadratum possess mostly dihydroxyacetone kinase genes while Salinibacter possesses mostly glycerol-3-phosphate dehydrogenase genes. Family abundance of genes dhaL and dhaK, phylogenetic analysis. Across gene family, taxonomic affiliations of the dihydroxyacetone kinase families are closest to each other, as well as those of the alcohol dehydrogenase (Fe-ADH) and glycerol kinase (FGGY) gene families. Halorubrum associates with dihydroxyacetone kinase gene families in the IC21 and Cahuil metagenomes. By using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
-
evolution
-
analysis of the glycerol metabolism genes in metagenomes suggests that Halorubrum and Haloquadratum possess mostly dihydroxyacetone kinase genes while Salinibacter possesses mostly glycerol-3-phosphate dehydrogenase genes. Family abundance of genes dhaL and dhaK, phylogenetic analysis. Across gene family, taxonomic affiliations of the dihydroxyacetone kinase families are closest to each other, as well as those of the alcohol dehydrogenase (Fe-ADH) and glycerol kinase (FGGY) gene families. Haloquadratum associates with dihydroxyacetone kinase gene families in the SS19, SS33, and SS37 metagenomes. By using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
-
evolution
Haloquadratum walsbyi JCM 12705
-
analysis of the glycerol metabolism genes in metagenomes suggests that Halorubrum and Haloquadratum possess mostly dihydroxyacetone kinase genes while Salinibacter possesses mostly glycerol-3-phosphate dehydrogenase genes. Family abundance of genes dhaL and dhaK, phylogenetic analysis. Across gene family, taxonomic affiliations of the dihydroxyacetone kinase families are closest to each other, as well as those of the alcohol dehydrogenase (Fe-ADH) and glycerol kinase (FGGY) gene families. Haloquadratum associates with dihydroxyacetone kinase gene families in the SS19, SS33, and SS37 metagenomes. By using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
-
additional information
1-propanol production from glycerol is achieved by addition of the ATP-dependent dihydroxyacetone kinase gene to Escherichia coli harboring pKK_mde and pRSF_pduCDEGOQS, reconstruction of the 1,2-propanediol (1,2-PD) synthetic pathway (pKK_mde) in Escherichia coli, pathway overview
additional information
analysis of the reaction mechanism of the wild-type enzyme and the most active experimentally measured mutant (Glu526Lys) with polyphosphate as phosphoryl donor by use of hybrid quantum mechanics/molecular mechanics (QM/MM) potentials, with the QM region described by semiempirical and DFT methods. The initial coordinates of the protein and the phospholipid are taken from the X-ray structure of the apoform of enzyme DHAK from Citrobacter freundii (PDB ID 1UN8). The crystal structure contains two protein chains defined as chain A and chain B. Since the full structure is symmetric, a fragment of each chain is removed obtaining a two close domain structure where the chain A fragment corresponds to the DhaL domain, and the chain B to the DhaK-domain. Missing residues of the flexible loop of the L-domain are manually added within the help of Molden program. The coordinates of Dha and magnesium cations are taken from the PDB ID 1UN9 that corresponds to the Dha/ANP form. The ATP binding domain is a barrel composed by eight amphipathic alpha-helix stabilized by a lipid. The phosphate groups of the nucleotide are coordinated via two magnesium ions to the side-chain carboxyl groups of aspartates. Structure-function analysis, overview. Construction of the B3LYP/MM optimized structure corresponding to the transition state of the phosphoryl transfer step for the substrate-assisted mechanism obtained in the wild-type enzyme, and in the E526K mutant
additional information
biological plausibility of virus-host associations, overview. Map of virus-host interactions generated by aligning spacers detected with reference-guided methods in metagenomes SS13, SS19, SS33, SS37, IC21, and Cahuil/C34
additional information
B9LNV8; B9LNV9
biological plausibility of virus-host associations, overview. Map of virus-host interactions generated by aligning spacers detected with reference-guided methods in metagenomes SS13, SS19, SS33, SS37, IC21, and Cahuil/C34
additional information
-
biological plausibility of virus-host associations, overview. Map of virus-host interactions generated by aligning spacers detected with reference-guided methods in metagenomes SS13, SS19, SS33, SS37, IC21, and Cahuil/C34
-
additional information
-
biological plausibility of virus-host associations, overview. Map of virus-host interactions generated by aligning spacers detected with reference-guided methods in metagenomes SS13, SS19, SS33, SS37, IC21, and Cahuil/C34
-
additional information
Shimwellia blattae ATCC33430
-
1-propanol production from glycerol is achieved by addition of the ATP-dependent dihydroxyacetone kinase gene to Escherichia coli harboring pKK_mde and pRSF_pduCDEGOQS, reconstruction of the 1,2-propanediol (1,2-PD) synthetic pathway (pKK_mde) in Escherichia coli, pathway overview
-
additional information
-
biological plausibility of virus-host associations, overview. Map of virus-host interactions generated by aligning spacers detected with reference-guided methods in metagenomes SS13, SS19, SS33, SS37, IC21, and Cahuil/C34
-
additional information
Haloquadratum walsbyi JCM 12705
-
biological plausibility of virus-host associations, overview. Map of virus-host interactions generated by aligning spacers detected with reference-guided methods in metagenomes SS13, SS19, SS33, SS37, IC21, and Cahuil/C34
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Show AA Sequence and Transmembrane Helices (1570 entries)
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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 * 62245, recombinant enzyme, deduced from amino acid sequence
homodimer
each subunit is formed by two domains. The dihydroxyacetone (Dha) binding site is located in the DhaK-domain while the ATP binding site is in the DhaL-domain. In the dimer, the subunits are disposed in an anti-parallel way. Therefore, the DhaK-domain of one subunit is faced with the DhaL-domain of the other subunit. The ATP binding domain is a barrel composed by eight amphipathic alpha-helix stabilized by a lipid. The phosphate groups of the nucleotide are coordinated via two magnesium ions to the side-chain carboxyl groups of aspartates. Structure-function analysis, overview
trimer
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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
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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
trimer
enzyme exists of a small, a large, and a substrate binding subunit
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
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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
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
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-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
E526K
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
additional information
E526K
based on the use of hybrid quantum mechanics/molecular mechanics (QM/MM) potentials, with the QM region described by semiempirical and DFT methods, the reaction mechanism of the wild-type enzyme and the most active experimentally measured mutant (Glu526Lys) with polyphosphate as phosphoryl donor is explored to elucidate the origin of the activity of this mutant. The mutation favors a more adequate position of the polyphosphate in the active site for the following step, the chemical reaction, to take place. Structure-function analysis, overview
additional information
constitutive co-overexpression of gene gldA1 or dhaD1, encoding a glycerol dehydrogenase (Gldh), and gene dhaK, encoding dihydroxyacetone kinase, as a fused protein results in a significant payoff in cell growth and acetone-butanol-ethanol (ABE) production compared to expression of one Gldh. Overexpression of [(dhaD1 + gldA1) dhaK] improves butanol and ABE production by 70% and 50%, respectively, in the presence of 5 and 6 g/l furfural relative to the plasmid control. Constitutive overexpression of two Gldh [dhaD1 + gldA1] as a fused protein increases glycerol utilization by 43% relative to the plasmid control, thus, representing about 14% increase in glycerol consumption relative to overexpression of GldA1 or DhaD1 alone. With [(dhaD1 + gldA1) dhaK], 28.6% increase in glycerol utilization is observed (compared to 43% by dhaD1 + gldA1), relative to the plasmid control. Inability of recombinant Clostridium beijerinckii to metabolize glycerol as a sole substrate. Method development and evaluation, overview
additional information
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constitutive co-overexpression of gene gldA1 or dhaD1, encoding a glycerol dehydrogenase (Gldh), and gene dhaK, encoding dihydroxyacetone kinase, as a fused protein results in a significant payoff in cell growth and acetone-butanol-ethanol (ABE) production compared to expression of one Gldh. Overexpression of [(dhaD1 + gldA1) dhaK] improves butanol and ABE production by 70% and 50%, respectively, in the presence of 5 and 6 g/l furfural relative to the plasmid control. Constitutive overexpression of two Gldh [dhaD1 + gldA1] as a fused protein increases glycerol utilization by 43% relative to the plasmid control, thus, representing about 14% increase in glycerol consumption relative to overexpression of GldA1 or DhaD1 alone. With [(dhaD1 + gldA1) dhaK], 28.6% increase in glycerol utilization is observed (compared to 43% by dhaD1 + gldA1), relative to the plasmid control. Inability of recombinant Clostridium beijerinckii to metabolize glycerol as a sole substrate. Method development and evaluation, overview
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additional information
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constitutive co-overexpression of gene gldA1 or dhaD1, encoding a glycerol dehydrogenase (Gldh), and gene dhaK, encoding dihydroxyacetone kinase, as a fused protein results in a significant payoff in cell growth and acetone-butanol-ethanol (ABE) production compared to expression of one Gldh. Overexpression of [(dhaD1 + gldA1) dhaK] improves butanol and ABE production by 70% and 50%, respectively, in the presence of 5 and 6 g/l furfural relative to the plasmid control. Constitutive overexpression of two Gldh [dhaD1 + gldA1] as a fused protein increases glycerol utilization by 43% relative to the plasmid control, thus, representing about 14% increase in glycerol consumption relative to overexpression of GldA1 or DhaD1 alone. With [(dhaD1 + gldA1) dhaK], 28.6% increase in glycerol utilization is observed (compared to 43% by dhaD1 + gldA1), relative to the plasmid control. Inability of recombinant Clostridium beijerinckii to metabolize glycerol as a sole substrate. Method development and evaluation, overview
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additional information
by using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
additional information
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by using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
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additional information
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by using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
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additional information
Haloquadratum walsbyi JCM 12705
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by using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
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additional information
B9LNV8; B9LNV9
by using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
additional information
-
by using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts
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additional information
1-propanol production from glycerol is achieved by addition of the ATP-dependent dihydroxyacetone kinase gene to Escherichia coli strain BW38029 harboring pKK_mde and pRSF_pduCDEGOQS, reconstruction of the 1,2-propanediol (1,2-PD) synthetic pathway (pKK_mde), pathway overview
additional information
Shimwellia blattae ATCC33430
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1-propanol production from glycerol is achieved by addition of the ATP-dependent dihydroxyacetone kinase gene to Escherichia coli strain BW38029 harboring pKK_mde and pRSF_pduCDEGOQS, reconstruction of the 1,2-propanediol (1,2-PD) synthetic pathway (pKK_mde), pathway overview
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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
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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
nickel affinity column chromatography and Superdex 200 gel filtration
polyethylene glycol 6000, polyethyleneimine, DEAE-Sepharose, Sepharose CL-6B
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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 BL21(DE3) cells
expressed in Escherichia coli NM522 cells
expressed in Escherichia coli strain BL21(DE3) and in chloroplasts from Nicotiana tabacum cultivar Xanthi
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gene dhaK, functional recombinant expression in Escherichia coli strain BW38029
gene dhaK, recombinant expression in Clostridium beijerinckii, coexpression with gene gldA1, encoding a glycerol dehydrogenase (Gldh) from Clostridium pasteurianum
genes dhaL and dhaK, DNA and amino acid sequence determination and analysis phylogenetic analysis
overexpression in Escherichia coli
phylogenetic analysis
genes dhaL and dhaK, DNA and amino acid sequence determination and analysis phylogenetic analysis
genes dhaL and dhaK, DNA and amino acid sequence determination and analysis phylogenetic analysis
B9LNV8; B9LNV9
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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
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inactivation of the gene lin0370 causes 20fold-elevated expression level of the dhaK-2 gene
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inactivation of the gene lin0370 causes 20fold-elevated expression level of the dhaK-2 gene
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inactivation of the gene lin0370 causes 20fold-elevated expression level of the dhaK-2 gene
Listeria innocua CLIP 11262
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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 (O74192), Komagataella pastoris
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.
20
2480-2486
2001
Escherichia coli (P37349), Escherichia coli (P76014), Escherichia coli (P76015), Escherichia coli
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 (P37349), Escherichia coli (P76014), Escherichia coli (P76015), Escherichia coli
brenda
Molin, M.; Norbeck, J.; Blomberg, A.
Dihydroxyacetone kinases in Saccharomyces cerevisiae are involved in detoxification of dihydroxyacetone
J. Biol. Chem.
278
1415-1423
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 (P45510), Citrobacter freundii
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 (P37349), Escherichia coli
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
283-293
2005
Escherichia coli (P76015), Escherichia coli
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
J. Biol. Chem.
280
18321-18325
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
1682-1689
2005
Rattus norvegicus, Homo sapiens (Q3LXA3), Homo sapiens
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, no activity in Clostridium acetobutylicum, Clostridium butyricum VPI 3266, 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
539-545
2006
Escherichia coli (P76014), Escherichia coli
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
-
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
J. Bacteriol.
194
4972-4982
2012
Listeria innocua, Listeria monocytogenes, Listeria innocua CLIP 11262
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 (P76015), Escherichia coli
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.
-
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 (Q1KLC3), Citrobacter freundii, 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
Agu, C.; Ujor, V.; Ezeji, T.
Metabolic engineering of Clostridium beijerinckii to improve glycerol metabolism and furfural tolerance
Biotechnol. Biofuels
12
50
2019
Clostridium pasteurianum (A0A0H3J0E7), Clostridium pasteurianum ATCC 6013 (A0A0H3J0E7), Clostridium pasteurianum DSM 525 (A0A0H3J0E7)
brenda
Bordes, I.; Garcia-Junceda, E.; Sanchez-Moreno, I.; Castillo, R.; Moliner, V.
Computational study of the phosphoryl donor activity of dihydroxyacetone kinase from ATP to inorganic polyphosphate
Int. J. Quantum Chem.
118
e25520
2018
Citrobacter freundii (P45510)
-
brenda
Matsubara, M.; Urano, N.; Yamada, S.; Narutaki, A.; Fujii, M.; Kataoka, M.
Fermentative production of 1-propanol from D-glucose, L-rhamnose and glycerol using recombinant Escherichia coli
J. Biosci. Bioeng.
122
421-426
2016
Shimwellia blattae (A0A143T1M7), Shimwellia blattae ATCC33430 (A0A143T1M7)
brenda
Moller, A.G.; Liang, C.
Determining virus-host interactions and glycerol metabolism profiles in geographically diverse solar salterns with metagenomics
PeerJ
5
e2844
2017
Halorubrum lacusprofundi (B9LNV8 AND B9LNV9), Haloquadratum walsbyi (G0LLJ3 AND G0LLJ4), Haloquadratum walsbyi DSM 16854 (G0LLJ3 AND G0LLJ4), Halorubrum lacusprofundi ATCC 49239 (B9LNV8 AND B9LNV9), Haloquadratum walsbyi C23 (G0LLJ3 AND G0LLJ4), Haloquadratum walsbyi JCM 12705 (G0LLJ3 AND G0LLJ4)
brenda
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