Information on EC 2.5.1.92 - (2Z,6Z)-farnesyl diphosphate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.5.1.92
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RECOMMENDED NAME
GeneOntology No.
(2Z,6Z)-farnesyl diphosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + 2 isopentenyl diphosphate = 2 diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bergamotene biosynthesis II
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Biosynthesis of secondary metabolites
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Terpenoid backbone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 2 isopentenyl units)
This enzyme, originally characterized from wild tomato, specifically forms (2Z,6Z)-farnesyl diphosphate via neryl diphosphate and isopentenyl diphosphate. In wild tomato it is involved in the biosynthesis of several sesquiterpenes. See also EC 2.5.1.68 [(2Z,6E)-farnesyl diphosphate synthase] and EC 2.5.1.10 [(2E,6E)-farnesyl diphosphate synthase].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene PF3D7_1128400
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-
Manually annotated by BRENDA team
gene PF3D7_1128400
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-
Manually annotated by BRENDA team
gene SlCPT6
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
in Solanum habrochaites accession LA1393, enzyme zFPS catalyzes the formation of (2Z,6Z)-farnesyl diphosphate,Z,Z-FPP, which is subsequently cyclized by santalene/bergamotene synthase (SBS) to form several sesquiterpenes
physiological function
additional information
homology modeling and three-dimensional structure
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
dimethylallyl diphosphate + isopentenyl diphosphate
diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
neryl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
neryl diphosphate + isopentenyl diphosphate
diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
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-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
dimethylallyl diphosphate + isopentenyl diphosphate
diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
neryl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
risedronate
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competitive inhibitor
additional information
-
the enzyme is inhibited by nitrogen-containing bisphosphonates
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.16
dimethylallyl diphosphate
0.002 - 0.228
isopentenyl diphosphate
0.051
neryl diphosphate
pH 7.6, 30C, wild-type enzyme
additional information
additional information
-
Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.055
dimethylallyl diphosphate
0.066 - 0.19
isopentenyl diphosphate
0.069
neryl diphosphate
Solanum habrochaites
B8XA40
pH 7.6, 30C, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.92
dimethylallyl diphosphate
157
0.3 - 1.3
isopentenyl diphosphate
113
1.3
neryl diphosphate
Solanum habrochaites
B8XA40
pH 7.6, 30C, wild-type enzyme
1451
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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inhibition kinetics
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
type VI glandular trichome
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3+) pLys RIL by glutathione affinity chromatography to homogeneity
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in a bacterial expression vector with a poly-histidine tag located at the C terminus of the protein
gene PF3D7_1128400, DNA and amino acid sequence determination and analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3+) pLys RIL
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gene SlCPT6, located on chromosome 6, phylogenetic analysis, recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana mesophyll protoplasts
gene zFPS of the CPT1 locus, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional expression of codon-optimized synthetic version of CPT1 of accession LA1777, a monoterpene-producing accession, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D98E/S100Y/F107I
site-directed mutagenesis, mutant M3V1
D98E/S100Y/L106I/F107I
site-directed mutagenesis, mutant M4
S100Y/F107I
site-directed mutagenesis, mutant M2
S100Y/L106I/F107I
site-directed mutagenesis, mutant M3V2
additional information
change of 10 residues that correlate with changes in substrate in neryl diphosphate synthase, NDPS1, EC 2.5.1.28, from accession LA2409 to those found in zFPS, from accession LA1393 (Pro/Ser-45, which corresponds to the second residue in the predicted mature protein, is excluded), and reciprocal changes in zFPS (LA1393). The two resulting recombinant proteins are named NDPS1-M10 and zFPS-M10. The zFPS-M10 recombinant protein loses the ability to synthesize (2Z,6Z)-farnesyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate but gains NDPS1 activity and synthesizes neryl diphosphate at levels similar to enzyme NDPS1 from accession LA2409
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development