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Information on EC 2.5.1.85 - all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] and Organism(s) Arabidopsis thaliana and UniProt Accession Q8S948
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2.5.1.85 all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]IUBMB Comments
Geranylgeranyl diphosphate is preferred over farnesyl diphosphate as allylic substrate . The plant Arabidopsis thaliana has two different enzymes that catalyse this reaction. SPS1 contributes to the biosynthesis of the ubiquinone side-chain while SPS2 supplies the precursor of the plastoquinone side-chains .
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Word Map
- 2.5.1.85
- synthases
-
farnesyl
- isoprene
-
plastid
-
trypanosoma
-
isoprenoid
- ubiquinone-9
- plastoquinone-9
- plastochromanol-8
-
reoxidation
- lycopersicum
-
allylic
- cruzi
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
slsps, atsps2, tcspps, tbspps, at-sps1, at-sps2, atsps1, long-chain prenyl diphosphate synthase, long-chain solanesyl diphosphate synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SPS1
Sps2
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 5 isopentenyl units)
Geranylgeranyl diphosphate is preferred over farnesyl diphosphate as allylic substrate [1]. The plant Arabidopsis thaliana has two different enzymes that catalyse this reaction. SPS1 contributes to the biosynthesis of the ubiquinone side-chain while SPS2 supplies the precursor of the plastoquinone side-chains [2].
CAS REGISTRY NUMBER
COMMENTARY
83745-07-7
-
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
(2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + all-trans-nonaprenyl diphosphate
geranylgeranyl diphosphate is preferred over farnesyl diphosphate as allylic substrate
the main product is nonaprenyl diphosphate, considerable amounts of geranylgeranyl diphosphate are formed
-
?
dimethylallyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
(2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + all-trans-nonaprenyl diphosphate
At-SPS2 prefers geranylgeranyl diphosphate to farnesyl diphosphate as the allylic substrate
the main product is nonaprenyl diphosphate, considerable amounts of intermediates, such as geranylgeranyl diphosphate are formed
-
?
dimethylallyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
At-SPS1 contributes to the biosynthesis of the ubiquinone side-chain in Arabidopsis thaliana
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
At-SPS1 contributes to the biosynthesis of the ubiquinone side-chain in Arabidopsis thaliana
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
geranylgeranyl diphosphate is preferred over farnesyl diphosphate as allylic substrate
nonaprenyl diphosphate is almost exclusively formed
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
At-SPS1 contributes to the biosynthesis of the plastoquinone side-chain in Arabidopsis thaliana
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
At-SPS2 supplies the precursor of the plastoquinone side-chain in Arabidopsis thaliana
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
At-SPS2 prefers geranylgeranyl diphosphate to farnesyl diphosphate as the allylic substrate
a large amount of nonaprenyl diphosphate is formed
-
?
additional information
?
-
no activity with farnesyl diphosphate and dimethylallyl diphosphate
-
-
?
additional information
?
-
no activity with dimethylallyl diphosphate and geranyl diphosphate, recombinant His6-tagged At-SPS2 fusion protein and truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
-
-
?
additional information
?
-
no activity with dimethylallyl diphosphate and geranyl diphosphate, recombinant His6-tagged At-SPS2 fusion protein and truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
-
-
?
additional information
?
-
-
no activity with dimethylallyl diphosphate and geranyl diphosphate, recombinant His6-tagged At-SPS2 fusion protein and truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
-
-
?
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 + 8 isopentenyl diphosphate
8 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
dimethylallyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
At-SPS1 contributes to the biosynthesis of the ubiquinone side-chain in Arabidopsis thaliana
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
At-SPS1 contributes to the biosynthesis of the ubiquinone side-chain in Arabidopsis thaliana
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
At-SPS1 contributes to the biosynthesis of the plastoquinone side-chain in Arabidopsis thaliana
-
-
?
geranylgeranyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-nonaprenyl diphosphate
At-SPS2 supplies the precursor of the plastoquinone side-chain in Arabidopsis thaliana
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fibrillin 5B
FBN5-B, fibrillin 5B specifically interacts with solanesyl diphosphate synthase 1, which biosynthesize the solanesyl moiety of plastoquinone-9. Plants containing defective FBN5-B accumulate less plastoquinone-9 and its cyclized product, plastochromanol-8, but the levels of tocopherols are not affected. Homozygous mutations in FBN5 are seedling-lethal. FBN5-B is required for PQ-9 biosynthesis through its interaction with enzyme SPS. FBN5 binding to the hydrophobic solanesyl moiety, which is generated by SPS1, in FBN5 B/SPS homodimeric complexes stimulates the enzyme activity of SPS1
-
fibrillin 5B
FBN5-B, fibrillin 5B specifically interacts with solanesyl diphosphate synthase 2, which biosynthesize the solanesyl moiety of plastoquinone-9. Plants containing defective FBN5-B accumulate less plastoquinone-9 and its cyclized product, plastochromanol-8, but the levels of tocopherols are not affected. Homozygous mutations in FBN5 are seedling-lethal. FBN5-B is required for PQ-9 biosynthesis through its interaction with enzyme SPS. FBN5 binding to the hydrophobic solanesyl moiety, which is generated by SPS2, in FBN5 B/SPS homodimeric complexes stimulates the enzyme activity of SPS2
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00689
(2E,6E)-farnesyl diphosphate
pH 8.0, 30°C, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
0.00512
farnesyl diphosphate
pH 8.0, 30°C, His6-tagged At-SPS2 fusion protein
20
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: geranylgeranyl diphosphate
151
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: farnesyl diphosphate
0.000565
geranylgeranyl diphosphate
pH 8.0, 30°C, His6-tagged At-SPS2 fusion protein
0.000843
geranylgeranyl diphosphate
pH 8.0, 30°C, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus), truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
0.0289
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: geranylgeranyl diphosphate, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
0.0377
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: geranylgeranyl diphosphate, His6-tagged At-SPS2 fusion protein
0.182
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: farnesyl diphosphate, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
0.248
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: farnesyl diphosphate, His6-tagged At-SPS2 fusion protein
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.77
(2E,6E)-farnesyl diphosphate
pH 8.0, 30°C, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
2.33
geranylgeranyl diphosphate
pH 8.0, 30°C, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus), truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
14.7
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: farnesyl diphosphate
15
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: geranylgeranyl diphosphate
1.72
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: geranylgeranyl diphosphate, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
2.83
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: farnesyl diphosphate, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
547
(2E,6E)-farnesyl diphosphate
pH 8.0, 30°C, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
2770
geranylgeranyl diphosphate
pH 8.0, 30°C, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus), truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
0.0968
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: farnesyl diphosphate
0.752
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: geranylgeranyl diphosphate
15.5
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: farnesyl diphosphate, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
595
isopentenyl diphosphate
pH 8.0, 30°C, cosubstrate: geranylgeranyl diphosphate, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
co-expression network of the Arabidopsis thaliana solanesyl-diphosphate synthase family
malfunction
metabolism
physiological function
evolution
co-expression network of the Arabidopsis thaliana solanesyl-diphosphate synthase family
malfunction
metabolism
physiological function
malfunction
in contrast to other plastochromanol-8 biosynthetic mutants, neither the single atsps knock-outs nor the atsps1 atsps2 double knock-out display any defects in tocopherols accumulation or germination
malfunction
knockout of genes AtSPS1 and AtSPS2 causes a reduction in plastoquinone-9 content in leaves, and the leaves exhibit light suppression of photosynthetic system II under high-intensity light
metabolism
the enzyme is involved in the biosynthesis of solanesyl diphosphate and plastoquinone-9. FBN5-B is required for plastoquinone-9 biosynthesis through its interaction with enzyme SPS
metabolism
the enzyme interacts with the plastid lipid binding protein fibrillin5 for synthesis of the solanesyl diphosphate tail in plastoquinone-9
physiological function
Arabidopsis thaliana SPS1-overexpressing lines are much more resistant to photooxidative stress than the wild-type, showing marked decreases in leaf bleaching, lipid peroxidation and PSII photoinhibition under excess light. Comparison of the SPS1 overexpressors with other prenyl quinone mutants indicates that the enhanced phototolerance of the former plants is directly related to their increased capacities for plastoquinone-9 biosynthesis, phenotype, overview
physiological function
plastid isoforms of solanesyl-diphosphate synthase catalyze the elongation of the prenyl side chain involved in the plastoquinone-9 and plastochromanol-8 biosynthesis, plastochromanol-8 originates from a subfraction of the non-photoactive pool of plastoquinone-9
physiological function
solanesyl diphosphate synthase, Sps, is a key enzyme in the metabolic pathways of solanesol and plastoquinone biosynthesis
malfunction
knockout of genes AtSPS1 and AtSPS2 causes a reduction in plastoquinone-9 content in leaves, and the leaves exhibit light suppression of photosynthetic system II under high-intensity light
malfunction
leaves of the atsps2 knock-out are devoid of plastochromanol-8 and display severe losses of both non-photoactive and photoactive plastoquinone-9, resulting in near complete photoinhibition at high light intensity. The photoinhibition is paralleled by significant damage to photosystem II but not to photosystem I. In contrast to other plastochromanol-8 biosynthetic mutants, neither the single atsps knock-outs nor the atsps1 atsps2 double knock-out display any defects in tocopherols accumulation or germination
metabolism
FBN5-B is required for plastoquinone-9 biosynthesis through its interaction with enzyme SPS
metabolism
the enzyme is involved in the biosynthesis of solanesyl diphosphate and plastoquinone-9
metabolism
the enzyme interacts with the plastid lipid binding protein fibrillin5 for synthesis of the solanesyl diphosphate tail in plastoquinone-9
physiological function
plastid isoforms of solanesyl-diphosphate synthase catalyze the elongation of the prenyl side chain involved in the plastoquinone-9 and plastochromanol-8 biosynthesis, plastochromanol-8 originates from a subfraction of the non-photoactive pool of plastoquinone-9
physiological function
solanesyl diphosphate synthase, Sps, is a key enzyme in the metabolic pathways of solanesol and plastoquinone biosynthesis
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). SPS1_ARATH
406
0
44468
Swiss-Prot
Chloroplast (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of a T-DNA insertion mutant SALK_126948 from gene At1g78510 encoding AtSPS1
additional information
construction of a T-DNA insertion mutant SALK_126948 from gene At1g78510 encoding AtSPS1
additional information
construction of a T-DNA insertion mutant SALK_064292 from gene At1g17050 encoding AtSPS2
additional information
construction of a T-DNA insertion mutant SALK_064292 from gene At1g17050 encoding AtSPS2
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged At-SPS2 fusion protein partially purified to about 10% purity, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus) is purified to about 90% purity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene AtSPS1, overexpressing of the plastoquinone-9 biosynthesis gene SPS1 in Arabidopsis thaliana generating plants that specifically accumulate plastoquinone-9 and its derivative plastochromanol-8
gene AtSPS1, phylogenetic analysis, recombinant expression of N-terminally GST-tagged enzyme in Nicotiana benthamiana epidermis cell endoplasmic reticulum using Agrobacterium tumefaciens strain C58C1 for transfection
heterologous expression of SPS1 allows the generation of UQ-9 in a decaprenyl diphosphate synthase-defective strain of fission yeast and also in wild-type Escherichia coli
heterologously expressed in Escherichia coli as as His6-tagged fusion protein
expression in Escherichia coli, His6-tagged At-SPS2 fusion protein and the truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)
gene AtSPS2, phylogenetic analysis, recombinant expression of N-terminally GST-tagged enzyme in Nicotiana benthamiana leaf chloroplasts using Agrobacterium tumefaciens strain C58C1 for transfection
heterologous expression of either SPS1 allows the generation of UQ-9 in a decaprenyl diphosphate synthase-defective strain of fission yeast and also in wild-type Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirooka, K.; Bamba, T.; Fukusaki, E.I.; Kobayashi, A.
Cloning and kinetic characterization of Arabidopsis thaliana solanesyl diphosphate synthase
Biochem. J.
370
679-686
2003
Arabidopsis thaliana (Q8S948)
Hirooka, K.; Izumi, Y.; An, C.I.; Nakazawa, Y.; Fukusaki, E.; Kobayashi, A.
Functional analysis of two solanesyl diphosphate synthases from Arabidopsis thaliana
Biosci. Biotechnol. Biochem.
69
592-601
2005
Arabidopsis thaliana (Q76FS5), Arabidopsis thaliana (Q8S948), Arabidopsis thaliana
Jun, L.; Saiki, R.; Tatsumi, K.; Nakagawa, T.; Kawamukai, M.
Identification and subcellular localization of two solanesyl diphosphate synthases from Arabidopsis thaliana
Plant Cell Physiol.
45
1882-1888
2004
Arabidopsis thaliana (Q76FS5), Arabidopsis thaliana (Q8S948)
Block, A.; Fristedt, R.; Rogers, S.; Kumar, J.; Barnes, B.; Barnes, J.; Elowsky, C.G.; Wamboldt, Y.; Mackenzie, S.A.; Redding, K.; Merchant, S.S.; Basset, G.J.
Functional modeling identifies paralogous solanesyl-diphosphate synthases that assemble the side chain of plastoquinone-9 in plastids
J. Biol. Chem.
288
27594-27606
2013
Arabidopsis thaliana (Q76FS5), Arabidopsis thaliana (Q8S948)
Yan, N.; Liu, Y.; Gong, D.; Du, Y.; Zhang, H.; Zhang, Z.
Solanesol: a review of its resources, derivatives, bioactivities, medicinal applications, and biosynthesis
Phytochem. Rev.
14
403-417
2015
Solanum lycopersicum, Arabidopsis thaliana (Q76FS5), Arabidopsis thaliana (Q8S948)
-
Kim, E.H.; Lee, Y.; Kim, H.U.
Fibrillin 5 is essential for plastoquinone-9 biosynthesis by binding to solanesyl diphosphate synthases in Arabidopsis
Plant Cell
27
2956-2971
2015
Arabidopsis thaliana (Q76FS5), Arabidopsis thaliana (Q8S948), Arabidopsis thaliana Col-0 (Q76FS5), Arabidopsis thaliana Col-0 (Q8S948)
Ksas, B.; Becuwe, N.; Chevalier, A.; Havaux, M.
Plant tolerance to excess light energy and photooxidative damage relies on plastoquinone biosynthesis
Sci. Rep.
5
10919
2015
Arabidopsis thaliana (Q8S948), Arabidopsis thaliana Col-0 (Q8S948)
Kim, E.H.; Lee, D.W.; Lee, K.R.; Jung, S.J.; Jeon, J.S.; Kim, H.U.
Conserved function of fibrillin5 in the plastoquinone-9 biosynthetic pathway in Arabidopsis and rice
Front. Plant Sci.
8
1197
2017
Arabidopsis thaliana (Q76FS5), Arabidopsis thaliana (Q8S948)
Kahlau, S.; Schroeder, F.; Freigang, J.; Laber, B.; Lange, G.; Passon, D.; Kleessen, S.; Lohse, M.; Schulz, A.; von Koskull-Doering, P.; Klie, S.; Gille, S.
Aclonifen targets solanesyl diphosphate synthase, representing a novel mode of action for herbicides
Pest Manag. Sci.
76
3377-3388
2020
Arabidopsis thaliana (Q76FS5), Arabidopsis thaliana (Q8S948)
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