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Literature summary for 2.5.1.1 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 2.5.1.1

Cloned(Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
isopentenyl diphosphate substrate inhibition Phaedon cochleariae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00084
-
 isopentenyl diphosphate fixed substrate dimethylallyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Co2+ Phaedon cochleariae
0.0116
-
 dimethylallyl diphosphate fixed substrate isopentenyl diphosphate (0.015 mM), pH and temperature not specified in the publication, metal cofactor: Co2+ Phaedon cochleariae
0.0118
-
 isopentenyl diphosphate fixed substrate dimethylallyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Mg2+ Phaedon cochleariae
1.103
-
 dimethylallyl diphosphate fixed substrate isopentenyl diphosphate (0.015 mM), pH and temperature not specified in the publication, metal cofactor: Mg2+ 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 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
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 + isopentenyl diphosphate Phaedon cochleariae the enzyme is involved in the biosynthesis of the monoterpenoid precursors needed for formation of the defensive compound chrysomelidial. Geranyl diphosphate is needed for the de novo synthesis of the cyclopentanoid monoterpene iridoids, defensive compounds that are produced during the entire larval stage of Phaedon cochleariae diphosphate + geranyl 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 + isopentenyl diphosphate the enzyme is involved in the biosynthesis of the monoterpenoid precursors needed for formation of the defensive compound chrysomelidial. Geranyl diphosphate is needed for the de novo synthesis of the cyclopentanoid monoterpene iridoids, defensive compounds that are produced during the entire larval stage of Phaedon cochleariae Phaedon cochleariae diphosphate + geranyl diphosphate
-
 ?
dimethylallyl diphosphate + 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 farnesyl diphosphate Phaedon cochleariae diphosphate + geranyl 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
0.573
-
 isopentenyl diphosphate fixed substrate dimethylallyl 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