2.5.1.90: all-trans-octaprenyl-diphosphate synthase
This is an abbreviated version!
For detailed information about all-trans-octaprenyl-diphosphate synthase, go to the full flat file.
Word Map on EC 2.5.1.90
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2.5.1.90
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ubiquinone
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isoprenoids
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polyprenyl
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decaprenylation
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menaquinone
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prenylates
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undecaprenyl
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geranyl
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isoprene
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hexaprenyl
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farnesyl-pp
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solanesyl
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chain-length
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ddxxd
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4-hydroxybenzoate
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dolichols
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coq
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polyisoprenoids
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dimethylallyl
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carbocation
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cis-prenyltransferase
- 2.5.1.90
- ubiquinone
-
isoprenoids
-
polyprenyl
-
decaprenylation
- menaquinone
-
prenylates
- undecaprenyl
-
geranyl
- isoprene
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hexaprenyl
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farnesyl-pp
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solanesyl
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chain-length
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ddxxd
- 4-hydroxybenzoate
- dolichols
- coq
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polyisoprenoids
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dimethylallyl
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carbocation
- cis-prenyltransferase
Reaction
Synonyms
C40-OPP, cel, gbs1789, IspB, long-chain C40 octaprenyl diphosphate synthase, long-chain trans-prenyltransferase, octaprenyl diphosphate synthase, octaprenyl pyrophosphate, octaprenyl pyrophosphate synthase, octaprenyl-diphosphate synthase, Opp, OPP synthase, OPP synthetase, OPPs, trans-prenyltransferase
ECTree
2.5.1.90 all-trans-octaprenyl-diphosphate synthaseAdvanced search results
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results (Engineering
Engineering on EC 2.5.1.90 - all-trans-octaprenyl-diphosphate synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A79Y
no activity. Cells harboring wild-type ispB and the A79Y mutant produce mainly ubiquinone-6, although the activity of the enzyme with the A79Y mutation is completely abolished. Although the A79Y mutant is functionally inactive, it can regulate activity upon forming a heterodimer with wild-type IspB, and this dimer formation is important for the determination of the isoprenoid chain length
F75A
resulting ubiquinone species are almost the same as those produced by the wild-type enzyme
I32V
resulting ubiquinone species are almost the same as those produced by the wild-type enzyme
K170A
mutant cannot be isolated, mutant protein does not retain functional activity
K170G
mutant cannot be isolated, mutant protein does not retain functional activity
L31V
resulting ubiquinone species are almost the same as those produced by the wild-type enzyme
R321A
normal growth at 30°C, no growth at 43°C, main product is ubiquinone-8
R321V
products are ubiquinone-6 and ubiquinone-7, slow growth at 43°C
Y37A
mutant cannot be isolated, mutant protein does not retain functional activity
Y61V
resulting ubiquinone species are almost the same as those produced by the wild-type enzyme
R321A
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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
A76Y
A76Y/S77F
F132A
F132A/L128A
steady-state activity 0.0008 per s. Product chain length C55, C60
F132A/L128A/I123A
steady-state activity 0.00066 per s. Produuct chain length C55 to C75
F132A/L128A/I123A/D62A
products reach C95, beyond the largest chain length generated by all known trans-prenyltransferases. Steady-state activity 0.00061 per s
V73Y
mutation leads to additional accumulation of C30 intermediate
additional information
A76Y
mutant produces only C20 cores instead of the C40 core of octaprenyl diphosphate
A76Y/S77F
mutant produces only C20 cores instead of the C40 core of octaprenyl diphosphate. The A76Y/S77F mutant synthesizes a larger amount of C20 than the A76Y mutant
F132A
steady-state activity 0.0051 per s. Product chain length C45 to C60
additional information
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
additional information
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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
additional information
residue D85 is the most important residue in the first DDXXD motif for both farnesyl diphosphate and isopentenyl diphosphate binding through an H-bond network involving R93 and R94, respectively, whereas R94, K45, R48, and H77 are responsible for isopentenyl binding by providing H-bonds and ionic interactions. K170 and T171 may stabilize the farnesyl carbocation intermediate to facilitate the reaction, whereas R93 and K225 may stabilize the catalytic base for HR proton abstraction after isopentenyl diphosphate condensation. K225 and K235 in a flexible loop may interact with farnesyl diphosphate when the enzyme becomes a closed conformation, which is therefore crucial for catalysis. Q208 is near the hydrophobic part of isopentenyl diphosphate and is important for isopentenyl diphosphate binding and catalysis
additional information
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residue D85 is the most important residue in the first DDXXD motif for both farnesyl diphosphate and isopentenyl diphosphate binding through an H-bond network involving R93 and R94, respectively, whereas R94, K45, R48, and H77 are responsible for isopentenyl binding by providing H-bonds and ionic interactions. K170 and T171 may stabilize the farnesyl carbocation intermediate to facilitate the reaction, whereas R93 and K225 may stabilize the catalytic base for HR proton abstraction after isopentenyl diphosphate condensation. K225 and K235 in a flexible loop may interact with farnesyl diphosphate when the enzyme becomes a closed conformation, which is therefore crucial for catalysis. Q208 is near the hydrophobic part of isopentenyl diphosphate and is important for isopentenyl diphosphate binding and catalysis
additional information
expression rescues an Escherichia coli chromosomal ispB disruptant
additional information
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expression rescues an Escherichia coli chromosomal ispB disruptant
additional information
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expression rescues an Escherichia coli chromosomal ispB disruptant
