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(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + all-trans-decaprenyl diphosphate
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + decaprenyl diphosphate
(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate
diphosphate + ?
(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate
diphosphate + octaprenyl diphosphate
-
-
plus, in decreasing order, nonaprenyl diphosphate, decaprenyl diphosphate, and heptaprenyl diphosphate
-
?
(2E,6Z)-farnesyl diphosphate + isopentenyl diphosphate
diphosphate + decaprenyl diphosphate
-
highest catalytic efficiency
plus smaller amounts of intermediiates with shorter chain length
-
?
all-E-geranylgeranyl diphosphate + isopentenyl diphosphate
diphosphate + all-trans-decaprenyl diphosphate
-
74% of the activity with (2E,6E)-farnesyl diphosphate
plus minor amounts of undecaprenyl diphosphate
-
?
dimethyl allyl diphosphate + isopentenyl diphosphate
diphosphate + ?
-
-
-
?
geranyl diphosphate + 6 isopentenyl diphosphate
diphosphate + all-trans-decaprenyl diphosphate
-
95% of the activity with E,E-farnesyl diphosphate
the relative amount of C50 and C55 products, i.e. decaprenyl diphosphate and undecaprenyl diphosphate, changes depending on the concentration of Mg2+. The ratio of the C50 and C55 product formed at 1 mM Mg2+ is 23:1
-
?
geranyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + all-trans-decaprenyl diphosphate
geranyl diphosphate + isopentenyl diphosphate
diphosphate + ?
geranyl diphosphate + isopentenyl diphosphate
diphosphate + all-trans-decaprenyl diphosphate
-
-
-
-
?
geranyl diphosphate + isopentenyl diphosphate
diphosphate + decaprenyl diphosphate
-
-
plus some farnesyl diphosphate
-
?
geranylgeranyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + all-trans-decaprenyl diphosphate
neryl diphosphate + isopentenyl diphosphate
diphosphate + nonaprenyl diphosphate
-
-
plus some farnesyl diphosphate
-
?
additional information
?
-
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + all-trans-decaprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + all-trans-decaprenyl diphosphate
a major intermediate product (GGPP) is produced during the consecutive condensation reaction starting from FPP and IPP, leading to the formation of the final product (DPP) by adding six more IPPs. The two-major step catalytic mechanism might be a biochemical feature of insect DPPSs
-
-
?
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + all-trans-decaprenyl diphosphate
best substrate
high product specificity for decaprenyl synthesis
-
?
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + all-trans-decaprenyl diphosphate
compared with other priming substrates examined (geranyl diphosphate, geranylgeranyl diphosphate), farnesyl diphosphate results in the highest values for the reaction rate and kcat/KM. Dimethylallyl diphosphate is not a suitable substrate
decaprenyl diphosphate is the major product, other prenyl diphosphates comprise only minor components
-
?
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + all-trans-decaprenyl diphosphate
-
high product specificity for decaprenyl synthesis
-
?
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + all-trans-decaprenyl diphosphate
key enzyme in synthesis of the decaprenyl tail in coenzyme Q10
-
-
?
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + all-trans-decaprenyl diphosphate
the enzyme catalyzes the consecutive condensation of isopentenyl diphosphate with allylic diphosphates to produce decaprenyl diphosphate, which is used for the side chain of ubiquinone Q10
-
-
?
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + all-trans-decaprenyl diphosphate
-
-
plus minor amounts of undecaprenyl diphosphate
-
?
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + all-trans-decaprenyl diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + decaprenyl diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
7 diphosphate + decaprenyl diphosphate
-
-
plus solanesyl diphosphate
-
?
(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate
diphosphate + ?
-
-
-
?
(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate
diphosphate + ?
-
-
-
?
(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate
diphosphate + ?
-
-
main products are decaprenyl diphosphate and solanesyl diphosphate
-
?
geranyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + all-trans-decaprenyl diphosphate
-
decaprenyl diphosphate is the major product, other prenyl diphosphates comprise only minor components
-
?
geranyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + all-trans-decaprenyl diphosphate
-
-
-
?
geranyl diphosphate + isopentenyl diphosphate
diphosphate + ?
-
-
-
?
geranyl diphosphate + isopentenyl diphosphate
diphosphate + ?
-
-
-
?
geranyl diphosphate + isopentenyl diphosphate
diphosphate + ?
-
-
main products are decaprenyl diphosphate and solanesyl diphosphate
-
?
geranylgeranyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + all-trans-decaprenyl diphosphate
-
decaprenyl diphosphate is the major product, other prenyl diphosphates comprise only minor components
-
?
geranylgeranyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + all-trans-decaprenyl diphosphate
-
-
-
?
additional information
?
-
no activity with dimethylallyl diphosphate
-
-
?
additional information
?
-
no activity with dimethylallyl diphosphate
-
-
?
additional information
?
-
catalyzes the addition of isopentenyl diphosphate to dimethyl allyl diphosphate, geranyl diphosphate, (2E,6E)-farnesyl diphosphate, and (2E,6E,10E)-geranylgeranyl diphosphate as priming substrates
-
-
?
additional information
?
-
-
catalyzes the addition of isopentenyl diphosphate to dimethyl allyl diphosphate, geranyl diphosphate, (2E,6E)-farnesyl diphosphate, and (2E,6E,10E)-geranylgeranyl diphosphate as priming substrates
-
-
?
additional information
?
-
-
no substrate: dimethylallyl diphosphate
-
-
?
additional information
?
-
-
no substrate: geranyl diphosphate, dimethylallyl diphosphate
-
-
?
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0.00006 - 0.084
(2E,6E)-farnesyl diphosphate
0.00007 - 0.04
(2E,6E,10E)-geranylgeranyl diphosphate
0.29
(2E,6Z)-farnesyl diphosphate
-
pH 7.9, 37°C
0.0029
all-E-geranylgeranyl diphosphate
-
pH 7.3, 37°C
0.005 - 0.49
geranyl diphosphate
0.0115
geranyl geranyl diphosphate
pH 7.5, 37°C
0.00007 - 0.00375
geranylgeranyl diphosphate
0.0138 - 0.089
isopentenyl diphosphate
0.029
neryl diphosphate
-
pH 7.9, 37°C
0.00006
(2E,6E)-farnesyl diphosphate
-
pH 7.3, 37°C
0.00014
(2E,6E)-farnesyl diphosphate
pH 7.5, 37°C, mutant enzyme A197V
0.00014
(2E,6E)-farnesyl diphosphate
mutant A197V, pH 7.5, 37°C
0.00016
(2E,6E)-farnesyl diphosphate
pH 7.5, 37°C, mutant enzyme G63F
0.00016
(2E,6E)-farnesyl diphosphate
mutant C63F, pH 7.5, 37°C
0.00033
(2E,6E)-farnesyl diphosphate
pH 7.5, 37°C, mutant enzyme F190W
0.00033
(2E,6E)-farnesyl diphosphate
mutant F190W, pH 7.5, 37°C
0.00038
(2E,6E)-farnesyl diphosphate
pH 7.5, 37°C, mutant enzyme F190A
0.00038
(2E,6E)-farnesyl diphosphate
mutant F190A, pH 7.5, 37°C
0.0005
(2E,6E)-farnesyl diphosphate
wild-type, pH 7.5, 37°C
0.0005
(2E,6E)-farnesyl diphosphate
pH 7.5, 37°C, wild-type enzyme
0.00063
(2E,6E)-farnesyl diphosphate
pH 7.5, 37°C, mutant enzyme G63A
0.00063
(2E,6E)-farnesyl diphosphate
mutant C63A, pH 7.5, 37°C
0.0007
(2E,6E)-farnesyl diphosphate
pH 7.5, 37°C, mutant enzyme A70V
0.0007
(2E,6E)-farnesyl diphosphate
mutant A70V, pH 7.5, 37°C
0.0015
(2E,6E)-farnesyl diphosphate
pH 7.5, 37°C, mutant enzyme A70G
0.0015
(2E,6E)-farnesyl diphosphate
mutant A70G, pH 7.5, 37°C
0.00275
(2E,6E)-farnesyl diphosphate
pH 7.5, 37°C, mutant enzyme N193A
0.00275
(2E,6E)-farnesyl diphosphate
mutant N193A, pH 7.5, 37°C
0.00863
(2E,6E)-farnesyl diphosphate
-
pH 7.5, 30°C
0.0131
(2E,6E)-farnesyl diphosphate
pH 7.5, 37°C
0.084
(2E,6E)-farnesyl diphosphate
-
pH 7.9, 37°C
0.00007
(2E,6E,10E)-geranylgeranyl diphosphate
mutant A197V, pH 7.5, 37°C
0.00009
(2E,6E,10E)-geranylgeranyl diphosphate
mutant A70V, pH 7.5, 37°C
0.00013
(2E,6E,10E)-geranylgeranyl diphosphate
mutant C63F, pH 7.5, 37°C
0.00024
(2E,6E,10E)-geranylgeranyl diphosphate
mutant F190W, pH 7.5, 37°C
0.00032
(2E,6E,10E)-geranylgeranyl diphosphate
wild-type, pH 7.5, 37°C
0.00036
(2E,6E,10E)-geranylgeranyl diphosphate
mutant F190A, pH 7.5, 37°C
0.00072
(2E,6E,10E)-geranylgeranyl diphosphate
mutant C63A, pH 7.5, 37°C
0.0024
(2E,6E,10E)-geranylgeranyl diphosphate
mutant A70G, pH 7.5, 37°C
0.00375
(2E,6E,10E)-geranylgeranyl diphosphate
mutant N193A, pH 7.5, 37°C
0.00418
(2E,6E,10E)-geranylgeranyl diphosphate
-
pH 7.5, 30°C
0.0115
(2E,6E,10E)-geranylgeranyl diphosphate
pH 7.5, 37°C
0.04
(2E,6E,10E)-geranylgeranyl diphosphate
-
pH 7.9, 37°C
0.005
geranyl diphosphate
-
pH 7.3, 37°C
0.007
geranyl diphosphate
pH 7.5, 37°C
0.007
geranyl diphosphate
wild-type, pH 7.5, 37°C
0.0185
geranyl diphosphate
pH 7.5, 37°C
0.49
geranyl diphosphate
-
pH 7.9, 37°C
0.00007
geranylgeranyl diphosphate
pH 7.5, 37°C, mutant enzyme A197V
0.00009
geranylgeranyl diphosphate
pH 7.5, 37°C, mutant enzyme A70V
0.00013
geranylgeranyl diphosphate
pH 7.5, 37°C, mutant enzyme G63F
0.00024
geranylgeranyl diphosphate
pH 7.5, 37°C, mutant enzyme F190W
0.00032
geranylgeranyl diphosphate
pH 7.5, 37°C
0.00036
geranylgeranyl diphosphate
pH 7.5, 37°C, mutant enzyme F190A
0.00072
geranylgeranyl diphosphate
pH 7.5, 37°C, mutant enzyme G63A
0.0024
geranylgeranyl diphosphate
pH 7.5, 37°C, mutant enzyme A70G
0.00375
geranylgeranyl diphosphate
pH 7.5, 37°C, mutant enzyme N193A
0.0138
isopentenyl diphosphate
pH 7.5, 37°C
0.089
isopentenyl diphosphate
-
pH 7.9, 37°C
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evolution
the enzyme contains six conserved motifs (from I to V), i.e., motif I (GKxxR), motif II (DDxxD(x)4RRG), motif III (GExxQ), motif IV (Y(x)6KT), motif V (FQLxDDxxD) and motif VI (K(x)4DxxxGxxTxPxL), occurring in all DPPS-1s examined, including insect, vertebrate, yeast and plant DPPS-1s, and bacterial DPPSs
malfunction
construction of an Schizosaccharomyces pombe dps-deficient strain. This disruptant is not able to synthesize ubiquinone and has no detectable decaprenyl diphosphate synthase activity. The Sschizosaccharomyces pombe dps-deficient strain could not grow on either rich medium supplemented with glycerol or on minimal medium supplemented with glucose. The dps-deficient strain requires cysteine or glutathione for full growth on the minimal medium. In addition, the dps-deficient strain is more sensitive to H2O2 and Cu2+ than the wild type
malfunction
pathogenic mutations in PDSS2 (PDSS2 encodes the second subunit of decaprenyl diphosphate synthase) causing primary CoQ10 deficiency in an infant with fatal Leigh syndrome and nephrotic syndrome
malfunction
the deletion mutant of dlp1 lacks the enzymatic activity of decaprenyl diphosphate synthase, does not produce ubiquinone-10 and has the typical ubiquinone-deficient Schizosaccharomyces pombe phenotypes, namely hypersensitivity to hydrogen peroxide, the need for antioxidants for growth on minimal medium and an elevated production of H2S. Both the dps1 and dlp1 mutants can generate ubiquinone when they are transformed with a bacterial decaprenyl diphosphate synthase, which functions in its host as a homodimer
physiological function
the enzyme catalyzes the consecutive condensation of isopentenyl diphosphate with allylic diphosphates to produce decaprenyl diphosphate, which is used for the side chain of ubiquinone Q10
physiological function
an dps1 disruptant strain is not able to synthesize ubiquinone and has no detectable decaprenyl diphosphate synthase activity. The dps-deficient strain cannot grow on either rich medium supplemented with glycerol or on minimal medium supplemented with glucose. The dps-deficient strain requires cysteine or glutathione for full growth on the minimal medium. The dps-deficient strain is more sensitive to H2O2 and Cu2+ than the wild type
physiological function
both genes DPS1 and DLP1 are required for decaprenyl diphosphate synthase activity. The deletion mutant of dlp1 lacks the enzymatic activity of decaprenyl diphosphate synthase, does not produce ubiquinone-10 and has the typical ubiquinone-deficient Schizosaccharomyces pombe phenotypes, namely hypersensitivity to hydrogen peroxide, the need for antioxidants for growth on minimal medium and an elevated production of H2S. Both the dps1 and dlp1 mutants can generate ubiquinone when they are transformed with a bacterial decaprenyl diphosphate synthase, which functions in its host as a homodimer
physiological function
the insect long-chain prenyl diphosphate synthase is responsible for the biosynthesis of the side-chain of ubiquinone-10, UQ-10, in Aphis gossypii
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heterodimer
1 * 46150, subunit 1/AgDPPS1 + 1 x 46740, subunit 2/AgDPPS2, sequence calculation
octamer
-
8 * 42700, SDS-PAGE and gel filtration
?
x * 38900, calculated from sequence
?
-
x * 38900, calculated from sequence
-
?
x * 38100, calculated from sequence
?
x * 38100, SDS-PAGE and calculated
?
x * 33898, calculated from sequence
?
x * 41000, SDS-PAGE of His-tagged recombinant protein
?
x * 37000, calculated from sequence
?
-
x * 37000, calculated from sequence
-
?
-
x * 45443, calculated
heterotetramer
heterotetramer of 2 DPS1 and 2 DLP1 subunits, both components are involved in determining the length of the ubiquinone side chain
heterotetramer
2 * 42047 (DSP1) + 2 * 32411 (DLP1), both DPS1 and DLPd1 are required for the enzymatic activity, calculated from sequence
homodimer
2 * 36400, calculated from sequence
homodimer
2 * 38960, calculated from sequence
tetramer
2 * Dps1 + 2 * Dlp1, gel filtration and calculated
tetramer
2 * Dps1 + 2 * Dlp1, heterotetramer
additional information
the two subunits are essential for the function of enzyme DPPS, since neither AgDPPS1 nor AgDPPS2 alone show catalytic activity
additional information
the two subunits are essential for the function of enzyme DPPS, since neither AgDPPS1 nor AgDPPS2 alone show catalytic activity
additional information
both Dps1 and Dlp1 are required for enzymatic activity
additional information
both Dps1 and Dlp1 are required for enzymatic activity
additional information
both Dps1 and Dlp1 are required for enzymatic activity
additional information
Escherichia coli octaprenyl diphosphate synthase IspB interacts with Schizosaccharomyces pombe decaprenyl diphosphate synthase Dps1 and D-less polyprenyl diphosphate synthase Dlp1, forming a high-molecular weight complex that stabilizes IspB
additional information
-
Escherichia coli octaprenyl diphosphate synthase IspB interacts with Schizosaccharomyces pombe decaprenyl diphosphate synthase Dps1 and D-less polyprenyl diphosphate synthase Dlp1, forming a high-molecular weight complex that stabilizes IspB
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D245E
significant decrease of activity
D245G
complete loss of activity
R321A
expression of Schizosaccharomyces pombe decaprenyl diphosphate synthase Dps1 or D-less polyprenyl diphosphate synthase Dlp1 recover the thermo-sensitive growth of an Escherichia coli ispB R321A mutant and restor IspB activity and production of coenzyme Q-8. IspB interacts with Dlp1 or Dps1, forming a high-molecular weight complex that stabilizes IspB, leading to full functionality
A197V
mainly heptaprenyl diphosphate is produced with smaller amounts of octaprenyl diphosphate and solanesyl diphosphate. Compared to wild-type enzyme the KM- and Vmax-values are altered
A197V
main products all-E-octaprenyl diphosphate and heptaprenyl diphosphate
A70G
a small amount of undecaprenyl diphosphate is produced with higher amounts of decaprenyl diphosphate. Compared to wild-type enzyme the KM- and Vmax-values are altered
A70G
main product is decaprenyl diphosphate with small amounts of undecaprenyl diphosphate
A70V
mainly heptaprenyl diphosphate is produced with smaller amounts of octaprenyl diphosphate and solanesyl diphosphate. Compared to wild-type enzyme the KM- and Vmax-values are altered
A70V
main product is all-E-heptaprenyl diphosphate
A70Y
complete loss of activity
A70Y
mutation completely abolishes the decaprenyl diphosphate synthase function, indicating that Ala70 is important for enzyme activity and the determination of the chain-length properties of DdsA
C63A
an even distribution in the amounts of the four products, heptaprenyl diphosphate, octaprenyl diphosphate, solanesyl diphosphate and decaprenyl diphosphate is observed. Compared to wild-type enzyme the KM- and Vmax-values are altered
C63A
main products all-E-octaprenyl diphosphate and all-E-solanesyl diphosphate
C63F
produces mostly geranylfarnesyl diphosphate and octaprenyl diphosphosphate. Compared to wild-type enzyme the KM- and Vmax-values are altered. Compared to wild-type enzyme the KM- and Vmax-values are altered
C63F
main products all-E-octaprenyl diphosphate and all-E-geranylfarnesyl diphosphate
F190A
mainly heptaprenyl diphosphate is produced with smaller amounts of octaprenyl diphosphate and solanesyl diphosphate. Compared to wild-type enzyme the KM- and Vmax-values are altered
F190A
main product is all-E-heptaprenyl diphosphate
F190W
mainly heptaprenyl diphosphate is produced with smaller amounts of octaprenyl diphosphate and solanesyl diphosphate. Compared to wild-type enzyme the KM- and Vmax-values are altered
F190W
main product is all-E-heptaprenyl diphosphate
N193A
an even distribution in the amounts of the four products, heptaprenyl diphosphate, octaprenyl diphosphate, solanesyl diphosphate and decaprenyl diphosphate is observed. Compared to wild-type enzyme the KM- and Vmax-values are altered
N193A
main product is decaprenyl diphosphate
additional information
-
recombinant Escherichia coli harboring the decaprenyl diphosphate synthase gene produces CoQ10 as well as CoQ8 and CoQ9. The recombinant Escherichia coli harboring only the decaprenyl diphosphate synthase gene produces 0.21 mg/l of CoQ10, whereas Escherichia coli coexpressing decaprenyl diphosphate synthase and 1-deoxy-D-xylulose 5-phosphate synthase produces 0.37 mg/l of CoQ10. The CoQ10 fraction is increased from 15.86% for only decaprenyl diphosphate synthase to 29.78% for coexpression of decaprenyl diphosphate synthase and 1-deoxy-D-xylulose 5-phosphate synthase
additional information
-
nineteen mutants of decaprenyl diphosphate synthase are generated and their production of ubiquinones is compared to that of the wild type protein
additional information
human DLP1 is not able to complement a Schizosaccharomyces dpl1 disruptant. Escherichia coli double transformants expressing human DPS1 and DLP1 produce coenzyme Q10, and an in vitro activity of decaprenyl diphosphate synthase can be verified. Expression in Escherichia coli of heterologous combinations, human DLP1 and mouse DPS1, generates both Q9 and Q10, indicating both components are involved in determining the ubiquinone side chain
additional information
human DLP1 is not able to complement a Schizosaccharomyces dpl1 disruptant. Escherichia coli double transformants expressing human DPS1 and DLP1 produce coenzyme Q10, and an in vitro activity of decaprenyl diphosphate synthase can be verified. Expression in Escherichia coli of heterologous combinations, human DLP1 and mouse DPS1, generates both Q9 and Q10, indicating both components are involved in determining the ubiquinone side chain
additional information
human DLP1 is not able to complement a Schizosaccharomyces dpl1 disruptant. Escherichia coli double transformants expressing human DPS1 and DLP1 produce coenzyme Q10, and an in vitro activity of decaprenyl diphosphate synthase can be verified. Expression in Escherichia coli of heterologous combinations, human DLP1 and mouse DPS1, generates both Q9 and Q10, indicating both components are involved in determining the ubiquinone side chain
additional information
human DPS1 is able to complement a Schizosaccharomyces dps1 disruptant. Escherichia coli transformants expressing human DPS1 produce only coenzyme Q8 of Escherichia coli origin, double transformants expressing human DPS1 and DLP1 produce Q10, and an in vitro activity of decaprenyl diphosphate synthase can be verified. Expression in Escherichia coli of heterologous combinations, human DPS1 and mouse DLP1, generates both Q9 and Q10, indicating both components are involved in determining the ubiquinone side chain
additional information
human DPS1 is able to complement a Schizosaccharomyces dps1 disruptant. Escherichia coli transformants expressing human DPS1 produce only coenzyme Q8 of Escherichia coli origin, double transformants expressing human DPS1 and DLP1 produce Q10, and an in vitro activity of decaprenyl diphosphate synthase can be verified. Expression in Escherichia coli of heterologous combinations, human DPS1 and mouse DLP1, generates both Q9 and Q10, indicating both components are involved in determining the ubiquinone side chain
additional information
human DPS1 is able to complement a Schizosaccharomyces dps1 disruptant. Escherichia coli transformants expressing human DPS1 produce only coenzyme Q8 of Escherichia coli origin, double transformants expressing human DPS1 and DLP1 produce Q10, and an in vitro activity of decaprenyl diphosphate synthase can be verified. Expression in Escherichia coli of heterologous combinations, human DPS1 and mouse DLP1, generates both Q9 and Q10, indicating both components are involved in determining the ubiquinone side chain
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coexpression of decaprenyl diphosphate synthase and 1-deoxy-D-xylulose 5-phosphate synthase in Escherichia coli
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DdsA is expressed successfully in Escherichia coli. Recombinant Escherichia coli synthesizes UQ-10 in addition to the endogenous production UQ-8
efficient production of coenzyme Q10 in rice by introducing the gene for decaprenyl diphosphate synthase into rice sugary and shrunken mutants
expressed under the control of an Escherichia coli constitutive promoter, CoQ10 rather than endogenous CoQ8 is biologically synthesized as the major coenzyme Q. Expression of the ddsA gene with low copy number leads to the accumulation of CoQ10 in batch fermentation. A high cell density in fed-batch fermentation of Escherichia coli BL21/pACDdsA increases the CoQ10 concentration
expression in Escherichia coli
expression in Escherichia coli, detecting UQ-10 in addition to innate UQ-8 in Escherichia coli
expression in Escherichia coli. Escherichia coli JM109 harboring the dps gene produces ubiquinone-10 in addition to endogenous ubiquinone-8
expression in Escherichia coli. Expression of the ddsA gene complements the lethality resulting from a defect in the octaprenyl diphosphate synthase gene of Escherichia coli and produces coenzyme Q10, indicating that coenzyme Q10 can substitute for the function of coenzyme Q8
expression in Escherichia coli. Wild-type Escherichia coli produces coenzyme Q8 and does not produce any coenzyme Q10. Recombinant Escherichia coli produces coenzyme Q10 in addition to coenzyme Q8
for biotechnological production of coenzyme Q10 in recombinant Escherichia coli, three genetic manipulations are performed: heterologous expression of decaprenyl diphosphate synthase (Dps) from Agrobacterium tumefaciens, deletion of endogenous octaprenyl diphosphate synthase (IspB), and overexpression of 1-deoxy-D-xylulose synthase (Dxs). Expression of the dps gene and deletion of the ispB gene in Escherichia coli BL21(DE3) DELTAispB/pAP1 allows production of CoQ10 only. Coexpression of the dxs gene increases the specific content of CoQ10
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gene AgDPPS1, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression of N-terminally GST-tagged enzyme in Escherichia coli strain BL21, coexpression with gene AgDPPS2
gene AgDPPS2, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression of N-terminally GST-tagged enzyme in Escherichia coli strain BL21, coexpression with gene AgDPPS1
genetic engineering of rice to produce CoQ10 using the gene for decaprenyl diphosphate synthase from Gluconobacter suboxydans. The production of CoQ9 is almost completely replaced with that of CoQ10, despite the presence of endogenous CoQ9 synthesis. DdsA designed to express at the mitochondria increases accumulation of total CoQ amount in seeds
the proteins Dps1 abd Dlp1 must be present simultaneously in Escherichia coli transformants before ubiquinone-10, which is produced by Schizosaccharomyces pombe but not by Escherichia coli, is generated. DLP1 and DPS1 form a heterotetramer in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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