BRENDA - Enzyme Database
show all sequences of 2.5.1.10

Metal ions control product specificity of isoprenyl diphosphate synthases in the insect terpenoid pathway

Frick, S.; Nagel, R.; Schmidt, A.; Bodemann, R.R.; Rahfeld, P.; Pauls, G.; Brandt, W.; Gershenzon, J.; Boland, W.; Burse, A.; Proc. Natl. Acad. Sci. USA 110, 4194-4199 (2013)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli after truncation of the signal sequence at the 5'-end of the coding region
Phaedon cochleariae
Inhibitors
Inhibitors
Commentary
Organism
Structure
geranyl diphosphate
-
Phaedon cochleariae
isopentenyl diphosphate
substrate inhibition
Phaedon cochleariae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
Commentary
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]
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
Commentary
Textmining
Phaedon cochleariae
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Phaedon cochleariae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
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
723664
Phaedon cochleariae
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
723664
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
723664
Phaedon cochleariae
diphosphate + (2E,6E)-farnesyl diphosphate
-
-
-
?
Subunits
Subunits
Commentary
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
Commentary
Organism
PcIDS1
-
Phaedon cochleariae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
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
Commentary
pI Value Maximum
pI Value
Phaedon cochleariae
calculated from sequence
-
8.63
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli after truncation of the signal sequence at the 5'-end of the coding region
Phaedon cochleariae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
geranyl diphosphate
-
Phaedon cochleariae
isopentenyl diphosphate
substrate inhibition
Phaedon cochleariae
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
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
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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 (protein specific)
Metals/Ions
Commentary
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] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Phaedon cochleariae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
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
723664
Phaedon cochleariae
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
723664
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
723664
Phaedon cochleariae
diphosphate + (2E,6E)-farnesyl diphosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
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
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Phaedon cochleariae
calculated from sequence
-
8.63
General Information
General Information
Commentary
Organism
physiological function
the enzyme is involved in the biosynthesis of the monoterpenoid precursors needed for formation of the defensive compound chrysomelidial
Phaedon cochleariae
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme is involved in the biosynthesis of the monoterpenoid precursors needed for formation of the defensive compound chrysomelidial
Phaedon cochleariae
Other publictions for EC 2.5.1.10
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
750676
Kumar
Terpene moiety enhancement by ...
Catharanthus roseus
Front. Plant Sci.
9
942
2018
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-
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1
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1
1
-
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-
737926
Sharifirad
Characterization of a farnesyl ...
Penicillium brevicompactum, Penicillium brevicompactum MUCL 19011
Biotechnol. Lett.
38
71-79
2016
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1
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2
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8
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2
1
1
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2
1
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1
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738477
Deng
Enhanced (S)-linalool producti ...
Actinidia arguta
J. Appl. Microbiol.
121
187-195
2016
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1
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1
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3
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737359
Schmidberger
Structural characterization of ...
Pseudomonas aeruginosa
Acta Crystallogr. Sect. D
71
721-731
2015
-
-
1
1
-
-
2
-
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1
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2
-
5
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1
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2
1
3
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1
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1
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2
2
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1
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1
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2
1
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-
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737821
Gritzalis
Probing the molecular and stru ...
Homo sapiens
Bioorg. Med. Chem. Lett.
25
1117-1123
2015
-
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17
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1
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2
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1
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17
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1
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1
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738069
Marzinzik
Discovery of novel allosteric ...
Homo sapiens
ChemMedChem
10
1884-1891
2015
-
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26
-
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1
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1
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1
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2
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23
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23
26
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1
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1
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738331
Su
Cloning and characterization o ...
Matricaria chamomilla var. recutita
Genet. Mol. Res.
14
349-361
2015
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1
-
-
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-
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2
1
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6
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1
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4
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1
1
2
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1
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1
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2
1
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1
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4
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1
1
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-
-
-
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-
1
1
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-
1
-
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739384
Richter
A small, differentially regula ...
Zea mays
Planta
241
1351-1361
2015
-
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2
1
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4
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1
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3
1
2
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2
1
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1
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3
1
-
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-
-
-
-
-
-
1
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1
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739414
Zhao
Molecular cloning and characte ...
Tripterygium wilfordii
PLoS ONE
10
e0125415
2015
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-
1
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1
2
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3
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1
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3
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2
1
4
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2
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2
2
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2
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6
-
-
2
2
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-
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-
2
1
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-
2
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739656
Ferriols
Cloning and characterization o ...
Rhizosolenia setigera, Rhizosolenia setigera CCMP1694
Sci. Rep.
5
10246
2015
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-
1
-
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1
4
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1
4
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6
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4
1
2
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4
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1
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Aripirala
Structural and thermodynamic b ...
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Upregulation of endogenous far ...
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1
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Alcaino
Functional characterization of ...
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Taxodione and arenarone inhibi ...
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Frick
Metal ions control product spe ...
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Discovery of thienopyrimidine- ...
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The N-terminus and the chain-l ...
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722094
Demoro
Bisphosphonate metal complexes ...
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Dalton Trans.
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2012
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15
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15
15
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Nagaki
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Rosso
Synthesis and biological evalu ...
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Thabet
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723705
Fischer
Identification of a lysine res ...
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Kim
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Molecular characterization of ...
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706667
Huang
Binding of nitrogen-containing ...
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721799
De Schutter
Novel bisphosphonate inhibitor ...
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723445
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Molecular cloning and expressi ...
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701943
Taban
Isolation and characterization ...
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Vandermoten
Structural features conferring ...
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Reduced expression of the meva ...
Homo sapiens
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705195
Nagaki
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Substrate specificities of far ...
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163-167
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Nagaki
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Substrate specificities of wil ...
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Nagaki
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Substrate specificities of far ...
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685599
Deprele
Farnesyl pyrophosphate synthas ...
Homo sapiens
Bioorg. Med. Chem. Lett.
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686762
Vandermoten
Characterization of a novel ap ...
Myzus persicae
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582
1928-1934
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691214
Szajnman
Synthesis and biological evalu ...
Toxoplasma gondii, Trypanosoma cruzi
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16
3283-3290
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704028
Lewis
Cloning and characterisation o ...
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705019
Mukkamala
Bisphosphonate inhibition of a ...
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2008
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Farnesyl diphosphate synthase: ...
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657438
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Farnesyl diphosphate synthase; ...
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Structural and functional role ...
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Prenyltransferase from human l ...
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Purification of farnesylpyroph ...
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Farnesyl pyrophosphate synthet ...
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Purification and characterizat ...
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The purification of prenyltran ...
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