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Information on EC 2.5.1.92 - (2Z,6Z)-farnesyl diphosphate synthase and Organism(s) Solanum habrochaites and UniProt Accession B8XA40

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EC Tree
IUBMB 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].
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Solanum habrochaites
UNIPROT: B8XA40
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The taxonomic range for the selected organisms is: Solanum habrochaites
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
trans-isoprenyl diphosphate synthase, slcpt6, z,z-farnesyl diphosphate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cis,cis-farnesyl diphosphate synthase
-
Z,Z-farnesyl diphosphate synthase
-
Z,Z-farnesyl pyrophosphate synthase
-
Z,Z-FPP synthase
-
cis-prenyltransferase
-
-
Z,Z-farnesyl diphosphate synthase
-
-
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].
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
(2Z,6Z)-farnesyl diphosphate + 2 diphosphate
show the reaction diagram
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
show the reaction diagram
neryl diphosphate + isopentenyl diphosphate
diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
-
-
-
?
dimethylallyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
-
-
-
-
?
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
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-
?
NATURAL SUBSTRATE
NATURAL 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 + 2 isopentenyl diphosphate
2 diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.16
dimethylallyl diphosphate
0.108 - 0.228
isopentenyl diphosphate
0.051
neryl diphosphate
pH 7.6, 30°C, wild-type enzyme
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
pH 7.6, 30°C, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.92
dimethylallyl diphosphate
0.3 - 1.3
isopentenyl diphosphate
1.3
neryl diphosphate
pH 7.6, 30°C, wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
type VI glandular trichome
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
additional information
homology modeling and three-dimensional structure
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ZFPS_SOLHA
303
0
34430
Swiss-Prot
Chloroplast (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 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
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team