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ATP + acetol
ADP + acetol phosphate
-
i.e. 1-hydroxy-2-propanone
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
ATP + DL-glyceraldehyde
ADP + DL-glyceraldehyde 3-phosphate
-
D,L-glyceraldehyde binds strongly to the enzyme, slow product release
-
-
?
ATP + DL-glyceraldehyde
ADP + glyceraldehyde 3-phosphate
ATP + glycerone
ADP + glycerone phosphate
CTP + dihydroxyacetone
CDP + dihydroxyacetone phosphate
dihydroxyacetone + ATP
dihydroxyacetone phosphate + ADP
GTP + dihydroxyacetone
GDP + dihydroxyacetone phosphate
ITP + dihydroxyacetone
IDP + dihydroxyacetone phosphate
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
-
-
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone 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
-
?
UTP + dihydroxyacetone
UDP + dihydroxyacetone phosphate
additional information
?
-
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
-
-
-
-
?
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
Pelargonium sp.
-
-
-
-
?
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
-
-
-
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
-
-
-
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
-
-
-
?
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
-
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
i.e. dihydroxyacetone phosphate
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
-
ir
ATP + glycerone
ADP + glycerone phosphate
-
-
-
-
ir
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
-
?
ATP + glycerone
ADP + glycerone phosphate
dihydroxyacetone
-
-
?
ATP + glycerone
ADP + glycerone 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
-
?
dihydroxyacetone + ATP
dihydroxyacetone phosphate + ADP
-
-
-
?
dihydroxyacetone + ATP
dihydroxyacetone phosphate + ADP
-
-
-
-
?
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
?
-
-
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
?
-
-
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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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
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
-
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. 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
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
-
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
-
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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?
x * 59400, SDS-PAGE
?
x * 65300, deduced from nucleotide sequence
dimer
-
-
dimer
2 * 59500, isoenzyme Dak1
dimer
2 * 62000, recombinant enzyme, SDS-PAGE
dimer
2 * 62245, recombinant enzyme, deduced from amino acid sequence
dimer
-
2 * 71000, SDS-PAGE
dimer
-
2 * 71000, SDS-PAGE
-
homodimer
2 * 63000, SDS-PAGE
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
homodimer
-
2 * 63000, SDS-PAGE
-
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
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. 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
-
approx. 35000 Da, monomeric state is suggested
additional information
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
-
enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
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K382A
the mutant shows activity with polyphosphate
K514A
the mutant shows activity with polyphosphate
R207B
the mutant shows activity with polyphosphate
R475A
the mutant shows activity with polyphosphate
E526K
-
the mutant shows activity with polyphosphate
-
K382A
-
the mutant shows activity with polyphosphate
-
K514A
-
the mutant shows activity with polyphosphate
-
R207B
-
the mutant shows activity with polyphosphate
-
R475A
-
the mutant shows activity with polyphosphate
-
H169A
completely inactive
H439A
completely inactive
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
E526K
the mutant shows activity with polyphosphate
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
-
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
-
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
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
-
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
-
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
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
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
-
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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