Any feedback?
Information on EC 2.5.1.92 - (2Z,6Z)-farnesyl diphosphate synthase
for references in articles please use BRENDA:EC2.5.1.92Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.5.1.92 (2Z,6Z)-farnesyl diphosphate synthaseIUBMB Comments
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].
Specify your search results
Word Map
- 2.5.1.92
-
neryl
-
terpene
- tomato
-
trichomes
-
longer-chain
-
rnai-mediated
-
thermococcus
- kodakaraensis
- cis-prenyltransferases
- lycopersicum
- solanum
-
sesquiterpenes
- drug development
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
trans-isoprenyl diphosphate synthase, slcpt6, z,z-farnesyl diphosphate synthase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
short-chain cis-prenyldiphosphate synthase
short-chain SlCPT
SlCPT6
Z,Z-farnesyl diphosphate synthase
zFPS
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + 2 isopentenyl diphosphate = 2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + 2 isopentenyl diphosphate
(2Z,6Z)-farnesyl diphosphate + 2 diphosphate
head-to-middle condensation function is observed in the N-terminal truncated enzyme. High substrate specificity is demonstrated in this enzyme as the irregular function only occurs without the presence of isopentenyl diphosphate
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
neryl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
neryl diphosphate + isopentenyl diphosphate
diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
the product farnesyl diphosphate is an important precursor in the isoprenoid synthesis pathway
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
positive cooperativity for the binding of the enzyme to isopentenyl diphosphate
-
-
?
neryl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
?
neryl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
neryl diphosphate is the preferred acceptor substrate
-
-
?
neryl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
?
neryl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
neryl diphosphate is the preferred acceptor substrate
-
-
?
additional information
?
-
-
a bifunctional enzyme farnesyl diphosphate/geranylgeranyl diphosphate synthase exists in Plasmodium falciparum
-
-
?
additional information
?
-
-
the enzyme also performs the synthesis of (2E,6E)-farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate, reaction of EC 2.5.1.10, and of geranylgeranyl diphosphate from (2E,6E)-farnesyl diphosphate and isopentenyl diphosphate, reaction of EC 2.5.1.29. Product identification by thin layer chromatography and mass spectrometry
-
-
?
additional information
?
-
-
a bifunctional enzyme farnesyl diphosphate/geranylgeranyl diphosphate synthase exists in Plasmodium falciparum
-
-
?
additional information
?
-
-
the enzyme also performs the synthesis of (2E,6E)-farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate, reaction of EC 2.5.1.10, and of geranylgeranyl diphosphate from (2E,6E)-farnesyl diphosphate and isopentenyl diphosphate, reaction of EC 2.5.1.29. Product identification by thin layer chromatography and mass spectrometry
-
-
?
additional information
?
-
the relative positioning of aromatic amino acid residues at positions 100 and 107 determines the ability of these enzymes to synthesize neryl diphosphate or (2Z,6Z)-farnesyl diphosphate
-
-
?
additional information
?
-
-
product analysis by radio-TLC and GC-MS
-
-
?
additional information
?
-
product analysis by radio-TLC and GC-MS
-
-
?
additional information
?
-
product analysis by radio-TLC and GC-MS
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
neryl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
the product farnesyl diphosphate is an important precursor in the isoprenoid synthesis pathway
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
?
neryl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
?
neryl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
-
-
-
?
additional information
?
-
-
a bifunctional enzyme farnesyl diphosphate/geranylgeranyl diphosphate synthase exists in Plasmodium falciparum
-
-
?
additional information
?
-
-
a bifunctional enzyme farnesyl diphosphate/geranylgeranyl diphosphate synthase exists in Plasmodium falciparum
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme is inhibited by nitrogen-containing bisphosphonates
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics
-
0.01
dimethylallyl diphosphate
pH 7.8, 30°C, 0.035 mM isopentenyl diphosphate
0.01
dimethylallyl diphosphate
pH 7.8, 30°C, 0.18 mM isopentenyl diphosphate
0.035
dimethylallyl diphosphate
pH 7.8, 30°C, 0.21 mM isopentenyl diphosphate
0.068
dimethylallyl diphosphate
-
pH 7.5, 37°C, recombinant enzyme, with isopentenyl diphosphate
0.002
isopentenyl diphosphate
-
pH 7.5, 37°C, recombinant enzyme, with dimethylallyl diphosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
monoterpene-producing accession LA1393, gene zFPS of the CPT1 locus
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
the enzyme is constitutively expressed in all stages during the asexual intra-erythrocytic cycle of Plasmodium falciparum, overview
brenda
additional information
-
the enzyme is constitutively expressed in all stages during the asexual intra-erythrocytic cycle of Plasmodium falciparum, overview
-
brenda
additional information
-
enzyme SlCPT6 is exclusively expressed in red fruit and roots
brenda
additional information
enzyme SlCPT6 is exclusively expressed in red fruit and roots
brenda
additional information
-
enzyme SlCPT6 is exclusively expressed in red fruit and roots
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
evolution
all the short-chain CPT genes from tomato (SlCPT1, SlCPT2 and SlCPT6) are closely linked to terpene synthase gene clusters. Six of the seven tomato CPT genes, SlCPT1, SlCPT2, SlCPT4, SlCPT5, SlCPT6 and SlCPT7, are in phylogenetic group 1 of the CPT superfamily
evolution
biochemical evolution of terpene biosynthesis in the glandular trichomes of Solanum species, comparative sequence analysis and evolutionary relationship of neryl diphosphate synthase 1 (EC 2.5.1.28, NDPS1) and (2Z,6Z)-farnesyl diphosphate synthase, cDNAs from the CPT1 locus, phylogenetic analysis, overview
evolution
-
all the short-chain CPT genes from tomato (SlCPT1, SlCPT2 and SlCPT6) are closely linked to terpene synthase gene clusters. Six of the seven tomato CPT genes, SlCPT1, SlCPT2, SlCPT4, SlCPT5, SlCPT6 and SlCPT7, are in phylogenetic group 1 of the CPT superfamily
-
physiological function
-
the enzyme is a key enzyme in the metabolism of virtually all isoprenoids and it interconnects the 5-carbon moiety isoprenoid synthesis with the mid- or long-chained compound synthesis. The synthesis of farnesyl diphosphate and geranylgeranyl diphosphate is required for biosynthesis of ubiquinone, dolichol, carotenoids, menaquinone, tocopherol, and protein prenylation
physiological function
-
the enzyme is a key enzyme in the metabolism of virtually all isoprenoids and it interconnects the 5-carbon moiety isoprenoid synthesis with the mid- or long-chained compound synthesis. The synthesis of farnesyl diphosphate and geranylgeranyl diphosphate is required for biosynthesis of ubiquinone, dolichol, carotenoids, menaquinone, tocopherol, and protein prenylation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ZFPS_SOLHA
303
0
34430
Swiss-Prot
Chloroplast (Reliability: 3)
CPT6_SOLLC
285
0
32797
Swiss-Prot
other Location (Reliability: 5)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor diffusion method, the crystal structure is determined at 2.31 A resolution. The structure of GsFPPase shows a three-layered all alpha-helical fold and conserved functional domains similar to other prenyltransferases
-
sitting-drop vapor diffusion method at 18 °C. Crystal structure of N-terminal truncated enzyme lacking the N-terminal segment (residues 1-70) with the double mutations D71M and E75A is determined
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3+) pLys RIL by glutathione affinity chromatography to homogeneity
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
-
the enzyme possibly represents an attractive drug target for the development of selective inhibitors aiming the erythrocytic stages of Plasmodium falciparum and development of more potent bisphosphonate-based inhibitors selectivity targeting this key point of the plasmodial isoprenoid metabolism
drug development
-
the enzyme possibly represents an attractive drug target for the development of selective inhibitors aiming the erythrocytic stages of Plasmodium falciparum and development of more potent bisphosphonate-based inhibitors selectivity targeting this key point of the plasmodial isoprenoid metabolism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sallaud, C.; Rontein, D.; Onillon, S.; Jabe, F.; Duff, P.; Giacalone, C.; Thoraval, S.; Escoffier, C.; Herbette, G.; Leonhardt, N.; Causse, M.; Tissier, A.
A novel pathway for sesquiterpene biosynthesis from Z,Z-farnesyl pyrophosphate in the wild tomato Solanum habrochaites
Plant Cell
21
301-317
2009
Solanum habrochaites (B8XA40)
brenda
Akhtar, T.A.; Matsuba, Y.; Schauvinhold, I.; Yu, G.; Lees, H.A.; Klein, S.E.; Pichersky, E.
The tomato cis-prenyltransferase gene family
Plant J.
73
640-652
2013
Solanum lycopersicum, Solanum lycopersicum (K7W9N9), Solanum lycopersicum MP-1 (K7W9N9)
brenda
Surmacz, L.; Plochocka, D.; Kania, M.; Danikiewicz, W.; Swiezewska, E.
cis-Prenyltransferase atCPT6 produces a family of very short-chain polyisoprenoids in planta
Biochim. Biophys. Acta
1841
240-250
2014
Solanum habrochaites (B8XA40)
brenda
Jordao, F.M.; Gabriel, H.B.; Alves, J.M.; Angeli, C.B.; Bifano, T.D.; Breda, A.; de Azevedo, M.F.; Basso, L.A.; Wunderlich, G.; Kimura, E.A.; Katzin, A.M.
Cloning and characterization of bifunctional enzyme farnesyl diphosphate/geranylgeranyl diphosphate synthase from Plasmodium falciparum
Malar. J.
12
184
2013
Plasmodium falciparum, Plasmodium falciparum clone 3D7
brenda
Kang, J.H.; Gonzales-Vigil, E.; Matsuba, Y.; Pichersky, E.; Barry, C.S.
Determination of residues responsible for substrate and product specificity of Solanum habrochaites short-chain cis-prenyltransferases
Plant Physiol.
164
80-91
2014
Solanum habrochaites
brenda
Beran, F.; Rahfeld, P.; Luck, K.; Nagel, R.; Vogel, H.; Wielsch, N.; Irmisch, S.; Ramasamy, S.; Gershenzon, J.; Heckel, D.G.; Koellner, T.G.
Novel family of terpene synthases evolved from trans-isoprenyl diphosphate synthases in a flea beetle
Proc. Natl. Acad. Sci. USA
113
2922-2927
2016
Phyllotreta striolata (A0A140AZ58), Phyllotreta striolata
brenda
Samori, P.Y.; Makabe, K.; Ohya, N.; Hatano, B.; Murakami, S.; Kijima, T.
Role of Cys73 in the thermostability of farnesyl diphosphate synthase from Geobacillus stearothermophilus
3 Biotech
7
236
2017
Geobacillus stearothermophilus
brenda
Chan, Y.T.; Ko, T.P.; Yao, S.H.; Chen, Y.W.; Lee, C.C.; Wang, A.H.
Crystal structure and potential head-to-middle condensation function of a Z,Z-farnesyl diphosphate synthase
ACS Omega
2
930-936
2017
Solanum habrochaites (B8XA40)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.5.1.92)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
