Information on EC 2.5.1.87 - ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.5.1.87
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RECOMMENDED NAME
GeneOntology No.
ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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dolichol and dolichyl phosphate biosynthesis
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Terpenoid backbone biosynthesis
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dolichol and dolichyl phosphate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 1055 isopentenyl units)
The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated alpha-isoprene unit, which serves as a glycosyl carrier in protein glycosylation [1]. The yeast Saccharomyces cerevisiae has two different enzymes that catalyse this reaction. Rer2p synthesizes a well-defined family of polyprenols of 13--18 isoprene residues with dominating C(80) (16 isoprene residues) extending to C(120), while Srt1p synthesizes mainly polyprenol with 22 isoprene subunits. Largest Srt1p products reach C(290) [2]. The enzyme from Arabidopsis thaliana catalyses the formation of polyprenyl diphosphates with predominant carbon number C(120) [4].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene rer2
UniProt
Manually annotated by BRENDA team
gene rer2
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
gene nus1
UNiProt
Manually annotated by BRENDA team
gene nus1
UNiProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate
13 diphosphate + di-trans,poly-cis-hexadecaprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + 14 isopentenyl diphosphate
14 diphosphate + di-trans,poly-cis-heptadecaprenyl diphosphate
show the reaction diagram
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di-trans,poly-cis-hexadecaprenyl diphosphate and di-trans,poly-cis-heptadecaprenyl diphosphate are the main products
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?
(2E,6E)-farnesyl diphosphate + 19 isopentenyl diphosphate
19 diphosphate + di-trans,poly-cis-docosaprenyl diphosphate
show the reaction diagram
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dominating polyprenol with 22 isoprene residues, Srt1p products reaching C290 indicate the failure of a strict bacterial-like chain length control
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?
(2E,6E)-farnesyl diphosphate + 21 isopentenyl diphosphate
21 diphosphate + di-trans,poly-cis tetracosaprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + di-trans,poly-cis-octaprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + di-trans,poly-cis-nonaprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate
diphosphate + di-trans,poly-cis-polyprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + dehydrodolichyl diphosphate
show the reaction diagram
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-
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
show the reaction diagram
dimethylallyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
show the reaction diagram
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weak activity
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-
?
geranyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
show the reaction diagram
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the enzyme preferably utilizes both geranyl diphosphate and farnesyl diphosphate as the starting substrate
Tk-IdsB produces cis-polyprenyl diphosphates ranging from C15 to C90. Above C75: 11.5%. C65C70: 60.7%. C55C60: 17.4%. C45C50: 3.3%. C30C40: 3.9%. Below C25: 3.2%, mainly yields the C60C65 products
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?
geranylgeranyl diphosphate + 20 isopentenyl diphosphate
20 diphosphate + di-trans,poly-cis-tetracosaprenyl diphosphate
show the reaction diagram
trans,trans-farnesyl diphosphate is a better substrate than geranylgeranyl diphosphate
the enzyme synthesizes polyisoprenes with carbon number higher than 90. The peak activity is observed at the point that corresponds to the polyisoprene with carbon number C120
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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
(2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate
13 diphosphate + di-trans,poly-cis-hexadecaprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + 14 isopentenyl diphosphate
14 diphosphate + di-trans,poly-cis-heptadecaprenyl diphosphate
show the reaction diagram
C7GM47
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di-trans,poly-cis-hexadecaprenyl diphosphate and di-trans,poly-cis-heptadecaprenyl diphosphate are the main products
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?
(2E,6E)-farnesyl diphosphate + 19 isopentenyl diphosphate
19 diphosphate + di-trans,poly-cis-docosaprenyl diphosphate
show the reaction diagram
P35196, Q03175
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dominating polyprenol with 22 isoprene residues, Srt1p products reaching C290 indicate the failure of a strict bacterial-like chain length control
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?
(2E,6E)-farnesyl diphosphate + 21 isopentenyl diphosphate
21 diphosphate + di-trans,poly-cis tetracosaprenyl diphosphate
show the reaction diagram
O80458
trans,trans-farnesyl diphosphate is a better substrate than geranylgeranyl diphosphate. The enzyme catalyzes the formation of polyprenyl diphosphates with predominant carbon number C120. In vitro rubber biosynthesis analysis indicates that the Arabidopsis cis-prenyltransferase itself could not catalyze the formation of high molecular weight polyprenyl diphosphate such as natural rubber
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-
?
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + di-trans,poly-cis-octaprenyl diphosphate
show the reaction diagram
C7GM47
the polyprenol product of Srt1p is longer in chain length than that of Rer2p and is not sufficiently converted to dolichol and dolichyl phosphate, unlike that of Rer2p
di-trans,poly-cis-octaprenyl diphosphate and di-trans,poly-cis-nonaprenyl diphosphate are the main products
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?
(2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + di-trans,poly-cis-nonaprenyl diphosphate
show the reaction diagram
C7GM47
the polyprenol product of Srt1p is longer in chain length than that of Rer2p and is not sufficiently converted to dolichol and dolichyl phosphate, unlike that of Rer2p
di-trans,poly-cis-octaprenyl diphosphate and di-trans,poly-cis-nonaprenyl diphosphate are the main products
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?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
show the reaction diagram
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the enzyme preferably utilizes both geranyl diphosphate and farnesyl diphosphate as the starting substrate
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-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
show the reaction diagram
geranyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
show the reaction diagram
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the enzyme preferably utilizes both geranyl diphosphate and farnesyl diphosphate as the starting substrate
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCl
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0.4 M, more than 90% inhibition
Mg2+
no activity in absence of Mg2+. Rapid increase of enzyme activity with the addition of Mg2+ up 2 mM. Further addition of Mg2+ inhibits the activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxycholate
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microsomal enzyme and enzyme released from microsomes are maximally activated at 5 mM. In the absence of deoxycholate, the released enzyme is inactive, while the microsomal enzyme has significant activity
Triton X-100
not strictly dependent on TRiton X-100, maximum activity at 0.01% Triton X-100
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00013 - 0.0149
(2E,6E)-farnesyl diphosphate
0.0094
dimethylallyl diphosphate
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65C
0.00096
farnesyl diphosphate
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65C
0.00175
geranyl diphosphate
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65C
0.00362
geranylgeranyl diphosphate
pH 7.5, 30C
0.000532 - 0.111
isopentenyl diphosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
37
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.95
calculated from sequence
8.05
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression is anther-specific, gene is differentially expressed during microspore development in the anther. Expression both in the microspore and in the anther wall increases to the maximum level in the anther wall of 35 mm buds, at which stage the tapetum becomes highly active and secretory
Manually annotated by BRENDA team
detected at high levels in roots but hardly detected in flowers, leaves, stems and in suspension-cultured cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Srt1p resides mostly in lipid particles
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
x * 33000, calculated from sequence
35500
x * 35700, calculated, x * 35500, SDS-PAGE
35700
x * 35700, calculated, x * 35500, SDS-PAGE
38410
x * 38410, calculated from sequence
additional information
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gel filtration of the released enzyme gives a peak of dehydrodolichyl diphosphate synthase activity, which appears between 150000 Da and 50000 Da molecular mass markers
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
on the basis of Escherichia coli undecaprenyl diphosphate synthase crystallographic structure the yeast Rer2p model is constructed. In the model three amino acid residues inserted into the sequence corresponding to the floor region of the tunnel extends the bottom loop what results in the required increase of the tunnel volume. Thermal fluctuations of this loop occasionally create a hole in the tunnel floor, making escape of polyprenol omega end out of the tunnel possible what switches off the control mechanism of product length thereby allowing a practically unlimited elongation process leading to an exponential distribution of longer chain polyprenols
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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half-life: 46 min, half-life is prolonged by immobilization on silica beads to 156 min
96
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not completely denatured
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, presence of glycerol is indispensable
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4C, 5 days, 20% glycerol, more than 60% of enzyme activity is retained
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
expression in yeast strain SNH23-7D, the identity of the cloned enzyme is confirmed by functional complementation of a yeast mutant strain defective in dehydrodolichyl-diphosphates synthase activity
expression the gene in a yeast mutant strain SNH23-7D
functional expression in Saccaromyces cerevisiae nus1DELTA/rer2DELTA/srt1DELTA mutant strain
gene nus1, recombinant expression in the Saccharomyces cerevisiae triple deletion strain, nus1DELTA/rer2DELTA/srt1DELTA, functional complementation by recombinant expression of active Schizosaccharomyces pombe enzyme
gene rer2, DNA and amino acid sequence determination and analysis, recombinant expression in Saccharomyces cerevisiae strain KG219, expression of CaRER2 under control of the MET3 promoter in mutant strain JOS14
gene rer2, phylogenetic analysis, quantitative RT-PCR expression analysis, functional complementation of the yeast rer2DELTA dolichol mutant, production of dolichols in rer2DELTA strains expressing both SlCPT3 and SlCPTBP associating together in an enzyme complex, recombinant coexpression of C-terminally Myc-tagged SlCPT3 and FLAG-tagged SlCPTBP in Nicotiana benthamiana leaves using Agrobacterium tumefaciens strain LBA4404, recombinant expression of C-terminally Myc-tagged SlCPT3 in Escherichia coli
over-expression of SRT1 suppresses the growth and glycosylation defects of rer2; when GFP-RER2 is over-expressed under the TDH3 promoter in DELTArer2, a continuous endioplasmic reticulum pattern and some dots associated with the endoplasmic reticulum are observed in the early logarithmic phase
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overexpression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene is endogenously induced by gibberellin, its induction is independent of ethylene regulation
induced in the stationary phase; mainly expressed in the early logarithmic phase
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Rer2p is active in logarithmic phase, with dominating polyprenol with 16 isoprene residues; Srt1p is expressed in stationary phase with dominating polyprenol with 22 isoprene residues
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R290H
a naturally occuring NgBR R290H mutation leading to congenital disorder of glycosylation. cis-PTase activity and mannose incorporation into proteins is markedly lower in NgBR R290H fibroblasts compared to control, the NgBR R290H mutant is a loss of function mutation that affects cis-PTase function of NgBR without disrupting complex formation with hCIT or Nogo-B. The reduced cis-PTase activity in fibroblasts is manifested as altered dolichol profiles in the urine or serum as assessed by mass spectrometry of all carriers of the R290H mutation, phenotype, overview
E68A
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product distributions is shifted to longer region to give the C65C70 as the main products
K109A
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product distributions is shifted to longer region to give the C65C70 as the main products
L113A
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product distributions is shifted to longer region to give the C65C70 as the main products
additional information
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