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Literature summary for 2.5.1.10 extracted from

  • Frick, S.; Nagel, R.; Schmidt, A.; Bodemann, R.R.; Rahfeld, P.; Pauls, G.; Brandt, W.; Gershenzon, J.; Boland, W.; Burse, A.
    Metal ions control product specificity of isoprenyl diphosphate synthases in the insect terpenoid pathway (2013), Proc. Natl. Acad. Sci. USA, 110, 4194-4199.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.10

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli after truncation of the signal sequence at the 5'-end of the coding region Phaedon cochleariae

Inhibitors

Inhibitors Comment Organism Structure
geranyl diphosphate
-
 Phaedon cochleariae
isopentenyl diphosphate substrate inhibition Phaedon cochleariae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0012
-
 geranyl diphosphate fixed substrate isopentenyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Mg2+ Phaedon cochleariae
0.0015
-
 isopentenyl diphosphate fixed substrate geranyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Co2+ Phaedon cochleariae
0.007
-
 isopentenyl diphosphate fixed substrate geranyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Mg2+ Phaedon cochleariae
0.0243
-
 geranyl diphosphate fixed substrate isopentenyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Co2+ Phaedon cochleariae

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ with dimethylallyl diphosphate and isopentenyl diphosphate the enzyme is far more active with Co2+ as an additive than with any other tested metal ion. In the presence of Co2+ or Mn2+, with dimethylallyl diphosphate as a cosubstrate, the enzyme produces about 96% geranyl diphosphate and only 4% farnesyl diphosphate. In contrast, with Mg2+ as an additive, PcIDS1 produces 18% geranyl diphosphate and 82% farnesyl diphosphate Phaedon cochleariae
Mg2+ with the substrates dimethylallyl diphosphate and isopentenyl diphosphate the enzyme is far more active with Co2+ as an additive than with any other tested metal ion. In the presence of Co2+ or Mn2+, with dimethylallyl diphosphate as a cosubstrate, the enzyme produces about 96% geranyl diphosphate and only 4% farnesyl diphosphate. In contrast, with Mg2+ as an additive, PcIDS1 produces 18% geranyl diphosphate and 82% farnesyl diphosphate. The production of farnesyl diphosphate from dimethylallyl diphosphate and geranyl diphosphate is most active by addition of 0.5 mM Mg2+ compared with any other tested cofactor. At a constant 0.5 mM Co2+, and an ascending Mg2+ concentration, PcIDS1 displayed low farnesyl diphosphate forming activity. If Mg2+ is constant at 5 mM and Co2+ concentrations vary, high farnesyl diphosphate production can be observed only at Co2+ concentrations below 0.1 mM. As soon as the Co2+ concentration ascends, the farnesyl diphosphate-forming activity decreases dramatically. The Mg2+-catalyzed activity of the enzyme is abolished as soon as Co2+ reaches its optimal concentration Phaedon cochleariae
additional information the enzyme is inactive without adding divalent metal cations Phaedon cochleariae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45800
-
 2 * 45800, the enzyme is always present as a dimer regardless of the added cofactor, in the case of Mg2+, the dimeric protein possesses the largest volume (93800 Da), most likely due to a more relaxed conformation. With Co2+, the enzyme seems to have a more compact conformation (87600 Da), which may be responsible for the change in product spectrum calculated from sequence Phaedon cochleariae
87600
-
 enzyme-Co2+ complex, gel filtration Phaedon cochleariae
93800
-
 enzyme-Mg2+ complex, gel filtration Phaedon cochleariae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylallyl diphosphate + geranyl diphosphate Phaedon cochleariae the enzyme is involved in the biosynthesis of the monoterpenoid precursors needed for formation of the defensive compound chrysomelidial. Farnesyl diphosphate serves as precursor for various primary metabolites and juvenile required hormone diphosphate + (2E,6E)-farnesyl diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Phaedon cochleariae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Phaedon cochleariae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylallyl diphosphate + 2 isopentenyl diphosphate the enzyme is bifunctional and produces (2E,6E)-farnesyl diphosphate or geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate depending on the divalent metal cofactor present. The enzyme is far more active with Co2+ as an additive than with any other tested metal ion. In the presence of Co2+ or Mn2+, with dimethylallyl diphosphate as a cosubstrate, it produces about 96% geranyl diphosphate and only 4% farnesyl diphosphate. In contrast, with Mg2+ as an additive, the enzyme produces 18% geranyl diphosphate and 82% farnesyl diphosphate Phaedon cochleariae 2 diphosphate + (2E,6E)-farnesyl diphosphate
-
 ?
dimethylallyl diphosphate + geranyl diphosphate the enzyme is involved in the biosynthesis of the monoterpenoid precursors needed for formation of the defensive compound chrysomelidial. Farnesyl diphosphate serves as precursor for various primary metabolites and juvenile required hormone Phaedon cochleariae diphosphate + (2E,6E)-farnesyl diphosphate
-
 ?
dimethylallyl diphosphate + geranyl diphosphate the production of farnesyl diphosphate from dimethylallyl diphosphate and geranyl diphosphate is most active by addition of 0.5 mM Mg2+ compared with any other tested cofactor. At a constant 0.5 mM Co2+, and an ascending Mg2+ concentration, PcIDS1 displayed low farnesyl diphosphate forming activity. If Mg2+ is constant at 5 mM and Co2+ concentrations vary, high farnesyl diphosphate production can be observed only at Co2+ concentrations below 0.1 mM. As soon as the Co2+ concentration ascends, the farnesyl diphosphate-forming activity decreases dramatically. The Mg2+-catalyzed activity of the enzyme is abolished as soon as Co2+ reaches its optimal concentration Phaedon cochleariae diphosphate + (2E,6E)-farnesyl diphosphate
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 45800, the enzyme is always present as a dimer regardless of the added cofactor, in the case of Mg2+, the dimeric protein possesses the largest volume (93800 Da), most likely due to a more relaxed conformation. With Co2+, the enzyme seems to have a more compact conformation (87600 Da), which may be responsible for the change in product spectrum calculated from sequence Phaedon cochleariae

Synonyms

Synonyms Comment Organism
PcIDS1
-
 Phaedon cochleariae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.322
-
 geranyl diphosphate fixed substrate isopentenyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Mg2+ Phaedon cochleariae
1.05
-
 isopentenyl diphosphate fixed substrate geranyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Mg2+ Phaedon cochleariae

pI Value

Organism Comment pI Value Maximum pI Value
Phaedon cochleariae calculated from sequence
-
 8.63

General Information

General Information Comment Organism
physiological function the enzyme is involved in the biosynthesis of the monoterpenoid precursors needed for formation of the defensive compound chrysomelidial Phaedon cochleariae