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Literature summary extracted from

  • Okada, K.; Kainou, T.; Tanaka, K.; Nakagawa, T.; Matsuda, H.; Kawamukai, M.
    Molecular cloning and mutational analysis of the ddsA gene encoding decaprenyl diphosphate synthase from Gluconobacter suboxydans (1998), Eur. J. Biochem., 255, 52-59.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.5.1.91 additional information no stimulation by K+, NH4+, Na+ Gluconobacter oxydans
2.5.1.91 Triton X-100 0.05% significantly activates, detergent is required Gluconobacter oxydans
2.5.1.91 Triton X-100 hardly any activity in absence of detergent. 0.05% required for full activity Gluconobacter oxydans
2.5.1.91 Tween 20 0.2% significantly activates, detergent is required Gluconobacter oxydans
2.5.1.91 Tween 20 hardly any activity in absence of detergent. 0.2% required for full activity Gluconobacter oxydans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.91 expression in Escherichia coli Gluconobacter oxydans
2.5.1.91 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 Gluconobacter oxydans

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.91 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 Gluconobacter oxydans
2.5.1.91 A197V main products all-E-octaprenyl diphosphate and heptaprenyl diphosphate Gluconobacter oxydans
2.5.1.91 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 Gluconobacter oxydans
2.5.1.91 A70G main product is decaprenyl diphosphate with small amounts of undecaprenyl diphosphate Gluconobacter oxydans
2.5.1.91 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 Gluconobacter oxydans
2.5.1.91 A70V main product is all-E-heptaprenyl diphosphate Gluconobacter oxydans
2.5.1.91 A70Y complete loss of activity Gluconobacter oxydans
2.5.1.91 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 Gluconobacter oxydans
2.5.1.91 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 Gluconobacter oxydans
2.5.1.91 C63A main products all-E-octaprenyl diphosphate and all-E-solanesyl diphosphate Gluconobacter oxydans
2.5.1.91 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 Gluconobacter oxydans
2.5.1.91 C63F main products all-E-octaprenyl diphosphate and all-E-geranylfarnesyl diphosphate Gluconobacter oxydans
2.5.1.91 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 Gluconobacter oxydans
2.5.1.91 F190A main product is all-E-heptaprenyl diphosphate Gluconobacter oxydans
2.5.1.91 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 Gluconobacter oxydans
2.5.1.91 F190W main product is all-E-heptaprenyl diphosphate Gluconobacter oxydans
2.5.1.91 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 Gluconobacter oxydans
2.5.1.91 N193A main product is decaprenyl diphosphate Gluconobacter oxydans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.91 0.00007
-
 geranylgeranyl diphosphate pH 7.5, 37°C, mutant enzyme A197V Gluconobacter oxydans
2.5.1.91 0.00007
-
 (2E,6E,10E)-geranylgeranyl diphosphate mutant A197V, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00009
-
 geranylgeranyl diphosphate pH 7.5, 37°C, mutant enzyme A70V Gluconobacter oxydans
2.5.1.91 0.00009
-
 (2E,6E,10E)-geranylgeranyl diphosphate mutant A70V, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00013
-
 geranylgeranyl diphosphate pH 7.5, 37°C, mutant enzyme G63F Gluconobacter oxydans
2.5.1.91 0.00013
-
 (2E,6E,10E)-geranylgeranyl diphosphate mutant C63F, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00014
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 37°C, mutant enzyme A197V Gluconobacter oxydans
2.5.1.91 0.00014
-
 (2E,6E)-farnesyl diphosphate mutant A197V, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00016
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 37°C, mutant enzyme G63F Gluconobacter oxydans
2.5.1.91 0.00016
-
 (2E,6E)-farnesyl diphosphate mutant C63F, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00024
-
 geranylgeranyl diphosphate pH 7.5, 37°C, mutant enzyme F190W Gluconobacter oxydans
2.5.1.91 0.00024
-
 (2E,6E,10E)-geranylgeranyl diphosphate mutant F190W, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00032
-
 geranylgeranyl diphosphate pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00032
-
 (2E,6E,10E)-geranylgeranyl diphosphate wild-type, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00033
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 37°C, mutant enzyme F190W Gluconobacter oxydans
2.5.1.91 0.00033
-
 (2E,6E)-farnesyl diphosphate mutant F190W, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00036
-
 geranylgeranyl diphosphate pH 7.5, 37°C, mutant enzyme F190A Gluconobacter oxydans
2.5.1.91 0.00036
-
 (2E,6E,10E)-geranylgeranyl diphosphate mutant F190A, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00038
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 37°C, mutant enzyme F190A Gluconobacter oxydans
2.5.1.91 0.00038
-
 (2E,6E)-farnesyl diphosphate mutant F190A, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.0005
-
 (2E,6E)-farnesyl diphosphate wild-type, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.0005
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 37°C, wild-type enzyme Gluconobacter oxydans
2.5.1.91 0.00063
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 37°C, mutant enzyme G63A Gluconobacter oxydans
2.5.1.91 0.00063
-
 (2E,6E)-farnesyl diphosphate mutant C63A, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.0007
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 37°C, mutant enzyme A70V Gluconobacter oxydans
2.5.1.91 0.0007
-
 (2E,6E)-farnesyl diphosphate mutant A70V, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00072
-
 geranylgeranyl diphosphate pH 7.5, 37°C, mutant enzyme G63A Gluconobacter oxydans
2.5.1.91 0.00072
-
 (2E,6E,10E)-geranylgeranyl diphosphate mutant C63A, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.0015
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 37°C, mutant enzyme A70G Gluconobacter oxydans
2.5.1.91 0.0015
-
 (2E,6E)-farnesyl diphosphate mutant A70G, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.0024
-
 geranylgeranyl diphosphate pH 7.5, 37°C, mutant enzyme A70G Gluconobacter oxydans
2.5.1.91 0.0024
-
 (2E,6E,10E)-geranylgeranyl diphosphate mutant A70G, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00275
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 37°C, mutant enzyme N193A Gluconobacter oxydans
2.5.1.91 0.00275
-
 (2E,6E)-farnesyl diphosphate mutant N193A, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.00375
-
 geranylgeranyl diphosphate pH 7.5, 37°C, mutant enzyme N193A Gluconobacter oxydans
2.5.1.91 0.00375
-
 (2E,6E,10E)-geranylgeranyl diphosphate mutant N193A, pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.007
-
 geranyl diphosphate pH 7.5, 37°C Gluconobacter oxydans
2.5.1.91 0.007
-
 geranyl diphosphate wild-type, pH 7.5, 37°C Gluconobacter oxydans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.91 Mg2+ 10 mM, required for full activity Gluconobacter oxydans
2.5.1.91 Mg2+ no activity below 5 mM. 10 mM required for full activity Gluconobacter oxydans
2.5.1.91 additional information not stimulated by monovalent cations such as NH4+, Na+ and K+ Gluconobacter oxydans
2.5.1.91 additional information no stimulation by K+, NH4+, Na+ Gluconobacter oxydans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.91 33898
-
 x * 33898, calculated from sequence Gluconobacter oxydans
2.5.1.91 41000
-
 x * 41000, SDS-PAGE of His-tagged recombinant protein Gluconobacter oxydans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.91 (2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate Gluconobacter oxydans 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 7 diphosphate + all-trans-decaprenyl diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.91 Gluconobacter oxydans O82832
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.91 His-tagged DdsA protein is purified Gluconobacter oxydans
2.5.1.91 recombinant enzyme Gluconobacter oxydans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.91 (2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
-
 Gluconobacter oxydans 7 diphosphate + all-trans-decaprenyl diphosphate
-
 ?
2.5.1.91 (2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate
-
 Gluconobacter oxydans 7 diphosphate + all-trans-decaprenyl diphosphate high product specificity for decaprenyl synthesis ?
2.5.1.91 (2E,6E)-farnesyl diphosphate + 7 isopentenyl 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 Gluconobacter oxydans 7 diphosphate + all-trans-decaprenyl diphosphate
-
 ?
2.5.1.91 (2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate
-
 Gluconobacter oxydans diphosphate + ?
-
 ?
2.5.1.91 geranyl diphosphate + 8 isopentenyl diphosphate
-
 Gluconobacter oxydans 8 diphosphate + all-trans-decaprenyl diphosphate
-
 ?
2.5.1.91 geranyl diphosphate + isopentenyl diphosphate
-
 Gluconobacter oxydans diphosphate + ?
-
 ?
2.5.1.91 geranylgeranyl diphosphate + 6 isopentenyl diphosphate
-
 Gluconobacter oxydans 6 diphosphate + all-trans-decaprenyl diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.91 ? x * 33898, calculated from sequence Gluconobacter oxydans
2.5.1.91 ? x * 41000, SDS-PAGE of His-tagged recombinant protein Gluconobacter oxydans

Synonyms

EC Number Synonyms Comment Organism
2.5.1.91 ddsa
-
 Gluconobacter oxydans
2.5.1.91 DdsA protein
-
 Gluconobacter oxydans
2.5.1.91 decaprenyl diphosphate synthase
-
 Gluconobacter oxydans
2.5.1.91 decaprenyl-PP synthase
-
 Gluconobacter oxydans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.91 40 45
-
 Gluconobacter oxydans
2.5.1.91 40 45 substrate: farnesyl diphosphate Gluconobacter oxydans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.91 7.5 8
-
 Gluconobacter oxydans

General Information

EC Number General Information Comment Organism
2.5.1.91 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 Gluconobacter oxydans