2.5.1.91: all-trans-decaprenyl-diphosphate synthase
This is an abbreviated version!
For detailed information about all-trans-decaprenyl-diphosphate synthase, go to the full flat file.
Word Map on EC 2.5.1.91
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2.5.1.91
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decaprenylation
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synthesis
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octaprenyl
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isoprenoid
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rhodobacter
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cosmetic
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solanesyl
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suboxydans
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sphingomonas
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geranyl
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fed-batch
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mevalonate
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synthases
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gluconobacter
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schizosaccharomyces
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pombe
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sphaeroides
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heteromer
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tumefaciens
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allyl
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agrobacterium
- 2.5.1.91
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decaprenylation
- synthesis
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octaprenyl
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isoprenoid
-
rhodobacter
-
cosmetic
-
solanesyl
- suboxydans
-
sphingomonas
-
geranyl
-
fed-batch
- mevalonate
- synthases
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gluconobacter
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schizosaccharomyces
- pombe
- sphaeroides
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heteromer
- tumefaciens
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allyl
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agrobacterium
Reaction
Synonyms
AgDPPS, D-less polyprenyl diphosphate synthase, Ddps, ddsa, DdsA protein, decaprenyl diphosphate synthase, decaprenyl diphosphate synthase 1, decaprenyl diphosphate synthase 2, decaprenyl diphosphate synthase gene, decaprenyl-PP synthase, DecPP synthase, decraprenyl diphosphate synthase, DLP1, Dps, DPS1, Rsdds
ECTree
2.5.1.91 all-trans-decaprenyl-diphosphate synthaseAdvanced search results
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results (Engineering
Engineering on EC 2.5.1.91 - all-trans-decaprenyl-diphosphate synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A197V
A70G
A70V
A70Y
C63A
C63F
F190A
F190W
N193A
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
additional information
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
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
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
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
additional information
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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
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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
