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Information on EC 2.5.1.87 - ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]
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2.5.1.87 ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]IUBMB Comments
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 . 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) . The enzyme from Arabidopsis thaliana catalyses the formation of polyprenyl diphosphates with predominant carbon number C(120) .
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Word Map
- 2.5.1.87
- dolichols
- cis-prenyltransferase
- pigmentosa
- dehydrodolichol
-
jewish
-
nogos
-
myoclonus
-
ashkenazi
- npc2
- polyprenols
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
dhdds, nogo-b receptor, rer2p, tk-idsb, srt1p, dedol-pp synthase, slcpt3, cis-ptase, dedolpp synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cis-prenyltransferase
cis-PTase
Dedol-PP synthase
dehydrodolichyl diphosphate synthase
NgBR
Nogo-B receptor
RER2
Rer2p
SlCPT3
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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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].
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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 + 13 isopentenyl diphosphate
13 diphosphate + di-trans,poly-cis-hexadecaprenyl diphosphate
(2E,6E)-farnesyl diphosphate + 14 isopentenyl diphosphate
14 diphosphate + di-trans,poly-cis-heptadecaprenyl diphosphate
-
di-trans,poly-cis-hexadecaprenyl diphosphate and di-trans,poly-cis-heptadecaprenyl diphosphate are the main products
-
?
(2E,6E)-farnesyl diphosphate + 19 isopentenyl diphosphate
19 diphosphate + di-trans,poly-cis-docosaprenyl diphosphate
-
dominating polyprenol with 22 isoprene residues, Srt1p products reaching C290 indicate the failure of a strict bacterial-like chain length control
-
?
(2E,6E)-farnesyl diphosphate + 21 isopentenyl diphosphate
21 diphosphate + di-trans,poly-cis tetracosaprenyl diphosphate
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + di-trans,poly-cis-octaprenyl diphosphate
(2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + di-trans,poly-cis-nonaprenyl diphosphate
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate
diphosphate + di-trans,poly-cis-polyprenyl diphosphate
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + dehydrodolichyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
dimethylallyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
-
weak activity
-
-
?
geranyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
-
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
-
?
geranylgeranyl diphosphate + 20 isopentenyl diphosphate
20 diphosphate + di-trans,poly-cis-tetracosaprenyl diphosphate
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
-
?
(2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate
13 diphosphate + di-trans,poly-cis-hexadecaprenyl diphosphate
-
di-trans,poly-cis-hexadecaprenyl diphosphate and di-trans,poly-cis-heptadecaprenyl diphosphate are the main products
-
?
(2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate
13 diphosphate + di-trans,poly-cis-hexadecaprenyl diphosphate
Rer2p Z-prenyltransferase synthesizes a well-defined family of polyprenols of 1318 isoprene residues with dominating C80 (16 isoprene residues) extending to C120. Two polyisoprenoid families with dominating C80 and C110 indicating the activity of both yeast Z-prenyltransferases Rer2p and Srt1p, respectively. The family of longer chain dolichols appearing in the stationary growth phase contains dolichols with even more than 50 isoprene units exhibiting monotonically decreasing amounts with increasing chain lengths. The family of shorter chain dolichols is characteristic of the Rer2p products synthesized during the logarithmic growth phase of yeast. It forms a well-defined family of dolichols with 1318 isoprene residues with a certain level of longer dolichols composed of up to 24 isoprene units
-
-
?
(2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate
13 diphosphate + di-trans,poly-cis-hexadecaprenyl diphosphate
Rer2p Z-prenyltransferase synthesizes a well-defined family of polyprenols of 1318 isoprene residues with dominating C80 (16 isoprene residues) extending to C120
-
-
?
(2E,6E)-farnesyl diphosphate + 21 isopentenyl diphosphate
21 diphosphate + di-trans,poly-cis tetracosaprenyl diphosphate
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
-
-
?
(2E,6E)-farnesyl diphosphate + 21 isopentenyl diphosphate
21 diphosphate + di-trans,poly-cis tetracosaprenyl diphosphate
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
-
?
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + di-trans,poly-cis-octaprenyl diphosphate
-
di-trans,poly-cis-octaprenyl diphosphate and di-trans,poly-cis-nonaprenyl diphosphate are the main products
-
?
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + di-trans,poly-cis-octaprenyl diphosphate
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
-
?
(2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + di-trans,poly-cis-nonaprenyl diphosphate
-
di-trans,poly-cis-octaprenyl diphosphate and di-trans,poly-cis-nonaprenyl diphosphate are the main products
-
?
(2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + di-trans,poly-cis-nonaprenyl diphosphate
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
-
?
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate
diphosphate + di-trans,poly-cis-polyprenyl diphosphate
-
chain length of products shifts downward from C90 and C95 with increasing concentration of the detergents. Maximum activation is observed at the concentration of 2% Triton X-100, 30 mM octyl glucoside, 30 mM 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate, and 10 mM deoxycholate with the product chain length being C80-C85, C65-C75, C70-C75, and C55-C65, respectively. The activity of Triton X-100 solubilized enzyme is decreased by asolectin, phosphatidylethanolamine, and phosphatidylcholine. The chain lengths of products formed in the presence of these phospholipids are C85 and C90. In the presence of both phosphatidylcholine and Mg2+ the solubilized enzyme is able to produce C90 and C95 dehydrodolichyl diphosphates like native microsomal enzyme
-
-
?
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate
diphosphate + di-trans,poly-cis-polyprenyl diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
-
the enzyme preferably utilizes both geranyl diphosphate and farnesyl diphosphate as the starting substrate
-
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
cis-prenyltransferase activity of the Candida albicans Rer2 homologue
n =10-55
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
cis-prenyltransferase activity of the Candida albicans Rer2 homologue
n =10-55
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
-
n = 10-55
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
-
n = 10-55
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
-
-
-
-
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
-
-
-
-
-
additional information
?
-
the enzyme does not need LEW1 as regulatory protein for its activity
-
-
-
additional information
?
-
the enzyme is responsible for the formation of long-chain dolichols, dolichol-18 to -23, with dolichol-21 dominating
-
-
-
additional information
?
-
dolichol synthesis using isopentenyl diphosphate
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-
?
additional information
?
-
dolichol synthesis using isopentenyl diphosphate
-
-
?
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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
(2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate
13 diphosphate + di-trans,poly-cis-hexadecaprenyl diphosphate
(2E,6E)-farnesyl diphosphate + 14 isopentenyl diphosphate
14 diphosphate + di-trans,poly-cis-heptadecaprenyl diphosphate
-
di-trans,poly-cis-hexadecaprenyl diphosphate and di-trans,poly-cis-heptadecaprenyl diphosphate are the main products
-
?
(2E,6E)-farnesyl diphosphate + 19 isopentenyl diphosphate
19 diphosphate + di-trans,poly-cis-docosaprenyl diphosphate
-
dominating polyprenol with 22 isoprene residues, Srt1p products reaching C290 indicate the failure of a strict bacterial-like chain length control
-
?
(2E,6E)-farnesyl diphosphate + 21 isopentenyl diphosphate
21 diphosphate + di-trans,poly-cis tetracosaprenyl diphosphate
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
-
-
?
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + di-trans,poly-cis-octaprenyl diphosphate
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
-
?
(2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + di-trans,poly-cis-nonaprenyl diphosphate
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
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
-
the enzyme preferably utilizes both geranyl diphosphate and farnesyl diphosphate as the starting substrate
-
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
geranyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
-
the enzyme preferably utilizes both geranyl diphosphate and farnesyl diphosphate as the starting substrate
-
-
?
(2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate
13 diphosphate + di-trans,poly-cis-hexadecaprenyl diphosphate
-
di-trans,poly-cis-hexadecaprenyl diphosphate and di-trans,poly-cis-heptadecaprenyl diphosphate are the main products
-
?
(2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate
13 diphosphate + di-trans,poly-cis-hexadecaprenyl diphosphate
Rer2p Z-prenyltransferase synthesizes a well-defined family of polyprenols of 1318 isoprene residues with dominating C80 (16 isoprene residues) extending to C120. Two polyisoprenoid families with dominating C80 and C110 indicating the activity of both yeast Z-prenyltransferases Rer2p and Srt1p, respectively. The family of longer chain dolichols appearing in the stationary growth phase contains dolichols with even more than 50 isoprene units exhibiting monotonically decreasing amounts with increasing chain lengths. The family of shorter chain dolichols is characteristic of the Rer2p products synthesized during the logarithmic growth phase of yeast. It forms a well-defined family of dolichols with 1318 isoprene residues with a certain level of longer dolichols composed of up to 24 isoprene units
-
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
cis-prenyltransferase activity of the Candida albicans Rer2 homologue
n =10-55
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
cis-prenyltransferase activity of the Candida albicans Rer2 homologue
n =10-55
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
-
n = 10-55
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate
-
n = 10-55
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
-
-
-
-
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
-
-
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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
Mg2+
-
required. Native microsomal enzyme exists in association with lipid and Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
deoxycholate
-
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
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Ataxia
A novel variant of dehydrodolichol diphosphate synthase (DHDDS) mutation with adult-onset progressive myoclonus ataxia.
Blindness
Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli.
Blindness
Purification and characterization of human dehydrodolychil diphosphate synthase (DHDDS) overexpressed in E. coli.
Blindness
Retinal Degeneration Caused by Rod-Specific Dhdds Ablation Occurs without Concomitant Inhibition of Protein N-Glycosylation.
Brain Diseases
De novo DHDDS variants cause a neurodevelopmental and neurodegenerative disorder with myoclonus.
Breast Neoplasms
Nogo-B receptor expression correlates negatively with malignancy grade and ki-67 antigen expression in invasive ductal breast carcinoma.
Breast Neoplasms
Nogo-B receptor increases the resistance of estrogen receptor positive breast cancer to paclitaxel.
Breast Neoplasms
Nogo-B receptor increases the resistance to tamoxifen in estrogen receptor-positive breast cancer cells.
Carcinogenesis
Nogo-B receptor increases the resistance to tamoxifen in estrogen receptor-positive breast cancer cells.
Carcinoma
Expression of Nogo isoforms and Nogo-B receptor (NgBR) in non-small cell lung carcinomas.
Carcinoma, Hepatocellular
A case of fatal Type I congenital disorders of glycosylation (CDG I) associated with low dehydrodolichol diphosphate synthase (DHDDS) activity.
Carcinoma, Hepatocellular
Nogo-B receptor promotes the chemoresistance of human hepatocellular carcinoma via the ubiquitination of p53 protein.
Carcinoma, Hepatocellular
The Nogo-B receptor promotes human hepatocellular carcinoma cell growth via the Akt signal pathway.
Carcinoma, Non-Small-Cell Lung
Nogo-B receptor is required for stabilizing TGF-? type I receptor and promotes the TGF-?1-induced epithelial-to-mesenchymal transition of non-small cell lung cancer.
Carcinoma, Non-Small-Cell Lung
Nogo-B receptor promotes epithelial-mesenchymal transition in non-small cell lung cancer cells through the Ras/ERK/Snail1 pathway.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation.
ditrans,polycis-polyprenyl diphosphate synthase [(2e,6e)-farnesyl diphosphate specific] deficiency
A case of fatal Type I congenital disorders of glycosylation (CDG I) associated with low dehydrodolichol diphosphate synthase (DHDDS) activity.
ditrans,polycis-polyprenyl diphosphate synthase [(2e,6e)-farnesyl diphosphate specific] deficiency
Nogo-B receptor deficiency causes cerebral vasculature defects during embryonic development in mice.
ditrans,polycis-polyprenyl diphosphate synthase [(2e,6e)-farnesyl diphosphate specific] deficiency
Nogo-B receptor deficiency increases liver X receptor alpha nuclear translocation and hepatic lipogenesis through an adenosine monophosphate-activated protein kinase alpha-dependent pathway.
Drug Resistant Epilepsy
Complex Neurological Phenotype Associated with a De Novo DHDDS Mutation in a Boy with Intellectual Disability, Refractory Epilepsy, and Movement Disorder.
Epilepsy, Generalized
A novel variant of dehydrodolichol diphosphate synthase (DHDDS) mutation with adult-onset progressive myoclonus ataxia.
Epilepsy, Generalized
Fifteen-year follow-up of a patient with a DHDDS variant with non-progressive early onset myoclonic tremor and rare generalized epilepsy.
Erectile Dysfunction
Silencing Nogo-B receptor inhibits penile corpus cavernosum vascular smooth muscle cell apoptosis of rats with diabetic erectile dysfunction by down-regulating ICAM-1.
Hyperkinesis
Complex Neurological Phenotype Associated with a De Novo DHDDS Mutation in a Boy with Intellectual Disability, Refractory Epilepsy, and Movement Disorder.
Hypertriglyceridemia
Activation of hepatic Nogo-B receptor expression-A new anti-liver steatosis mechanism of statins.
Intellectual Disability
Complex Neurological Phenotype Associated with a De Novo DHDDS Mutation in a Boy with Intellectual Disability, Refractory Epilepsy, and Movement Disorder.
Lung Neoplasms
Nogo-B receptor is required for stabilizing TGF-? type I receptor and promotes the TGF-?1-induced epithelial-to-mesenchymal transition of non-small cell lung cancer.
Lung Neoplasms
Nogo-B receptor promotes epithelial-mesenchymal transition in non-small cell lung cancer cells through the Ras/ERK/Snail1 pathway.
Melanoma
Prognostic Significance of NOGO-A/B and NOGO-B Receptor Expression in Malignant Melanoma - A Preliminary Study.
Movement Disorders
Complex Neurological Phenotype Associated with a De Novo DHDDS Mutation in a Boy with Intellectual Disability, Refractory Epilepsy, and Movement Disorder.
Myoclonus
A novel variant of dehydrodolichol diphosphate synthase (DHDDS) mutation with adult-onset progressive myoclonus ataxia.
Myoclonus
De novo DHDDS variants cause a neurodevelopmental and neurodegenerative disorder with myoclonus.
Neoplasm Metastasis
Delivery of small interfering RNA against Nogo-B receptor via tumor-acidity responsive nanoparticles for tumor vessel normalization and metastasis suppression.
Neoplasms
Correlation of Expression of CHI3L1 and Nogo-A and their Role in Angiogenesis in Invasive Ductal Breast Carcinoma.
Neoplasms
Delivery of small interfering RNA against Nogo-B receptor via tumor-acidity responsive nanoparticles for tumor vessel normalization and metastasis suppression.
Neoplasms
Nogo-B Receptor Directs Mitochondria-Associated Membranes to Regulate Vascular Smooth Muscle Cell Proliferation.
Neoplasms
Nogo-B receptor expression correlates negatively with malignancy grade and ki-67 antigen expression in invasive ductal breast carcinoma.
Neurodegenerative Diseases
De novo DHDDS variants cause a neurodevelopmental and neurodegenerative disorder with myoclonus.
Retinal Degeneration
Knock-Down DHDDS Expression Induces Photoreceptor Degeneration in Zebrafish.
Retinal Degeneration
Knockdown of Dehydrodolichyl Diphosphate Synthase in the Drosophila Retina Leads to a Unique Pattern of Retinal Degeneration.
Retinal Degeneration
Lack of Overt Retinal Degeneration in a K42E Dhdds Knock-In Mouse Model of RP59.
Retinal Degeneration
Mutation K42E in Dehydrodolichol Diphosphate Synthase (DHDDS) Causes Recessive Retinitis Pigmentosa.
Retinal Degeneration
Retinal Degeneration Caused by Rod-Specific Dhdds Ablation Occurs without Concomitant Inhibition of Protein N-Glycosylation.
Retinal Degeneration
Selective Ablation of Dehydrodolichyl Diphosphate Synthase in Murine Retinal Pigment Epithelium (RPE) Causes RPE Atrophy and Retinal Degeneration.
Retinal Diseases
Knockdown of Dehydrodolichyl Diphosphate Synthase in the Drosophila Retina Leads to a Unique Pattern of Retinal Degeneration.
Retinitis
De novo DHDDS variants cause a neurodevelopmental and neurodegenerative disorder with myoclonus.
Retinitis Pigmentosa
A missense mutation in DHDDS, encoding dehydrodolichyl diphosphate synthase, is associated with autosomal-recessive retinitis pigmentosa in Ashkenazi Jews.
Retinitis Pigmentosa
Aberrant dolichol chain lengths as biomarkers for retinitis pigmentosa caused by impaired dolichol biosynthesis.
Retinitis Pigmentosa
De novo DHDDS variants cause a neurodevelopmental and neurodegenerative disorder with myoclonus.
Retinitis Pigmentosa
Knockdown of Dehydrodolichyl Diphosphate Synthase in the Drosophila Retina Leads to a Unique Pattern of Retinal Degeneration.
Retinitis Pigmentosa
Lack of Overt Retinal Degeneration in a K42E Dhdds Knock-In Mouse Model of RP59.
Retinitis Pigmentosa
Mutation K42E in Dehydrodolichol Diphosphate Synthase (DHDDS) Causes Recessive Retinitis Pigmentosa.
Retinitis Pigmentosa
Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli.
Retinitis Pigmentosa
Purification and characterization of human dehydrodolychil diphosphate synthase (DHDDS) overexpressed in E. coli.
Retinitis Pigmentosa
Retinal Degeneration Caused by Rod-Specific Dhdds Ablation Occurs without Concomitant Inhibition of Protein N-Glycosylation.
Retinitis Pigmentosa
Two specific mutations are prevalent causes of recessive retinitis pigmentosa in North American patients of Jewish ancestry.
Retinitis Pigmentosa
Whole-exome sequencing links a variant in DHDDS to retinitis pigmentosa.
Status Epilepticus
Phenotype of heterozygous variants of dehydrodolichol diphosphate synthase.
Tremor
Fifteen-year follow-up of a patient with a DHDDS variant with non-progressive early onset myoclonic tremor and rare generalized epilepsy.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0149
(2E,6E)-farnesyl diphosphate
-
pH 8.5, 37°C, enzyme released from microsomes
0.00588
isopentenyl diphosphate
-
65°C, cosubstrate: geranyl diphosphate
0.0132
isopentenyl diphosphate
-
65°C, cosubstrate: farnesyl diphosphate
0.111
isopentenyl diphosphate
-
65°C, cosubstrate: dimethylallyl diphosphate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
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
brenda
expresses dehydrodolichyl diphosphate synthase mRNA at high levels
brenda
detected at high levels in roots but hardly detected in flowers, leaves, stems and in suspension-cultured cells
brenda
expresses dehydrodolichyl diphosphate synthase mRNA at high levels
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Srt1p resides mostly in lipid particles
-
brenda
localized to the continuous endoplasmic reticulum and some dots associated with the endoplasmic reticulum
brenda
peripheral but tightly associated membrane protein, localized to a subregion of the endoplasmic reticulum membrane that is specialized for dolichol synthesis
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
amino acid at 4th position from the C-terminus of NgBR is a functionally and evolutionary conserved residue
evolution
the class of enzymes known as cis-prenyltransferases (CPTs) elongate the trans-prenyl diphosphate intermediate with a cis-linked linear polymer of isopentenyl diphosphate units
evolution
-
the class of enzymes known as cis-prenyltransferases (CPTs) elongate the trans-prenyl diphosphate intermediate with a cis-linked linear polymer of isopentenyl diphosphate units
-
malfunction
rer2 mutant is defective in both N- and O-linked glycosylation in the endoplasmic reticulum, the rer2 mutant is deficient in the activity of cis-prenyltransferase, a key enzyme of dolichol synthesis
malfunction
the morphological differentiation of a Candida albicans cis-prenyltransferase mutant is impaired
malfunction
unique congenital disorder of glycosylation caused by a mutation in NgBR, a conserved subunit of cis-PTase. The disorder of glycosylation is caused by a loss-of-function mutation R290H in the conserved C-terminus of NgBR protein, fibroblasts isolated from patients exhibit reduced dolichol profiles. Mutation of NgBR-R290H in humans show the importance of the evolutionarily conserved residue R290 for mammalian cis-PTase activity and function
malfunction
unique congenital disorder of glycosylation caused by a mutation in NgBR, a conserved subunit of cis-PTase. The disorder of glycosylation is caused by a loss-of-function mutation R290H in the conserved C-terminus of NgBR protein, fibroblasts isolated from patients exhibit reduced dolichol profiles. Mutation of NgBR-R290H in humans show the importance of the evolutionarily conserved residue R290 for mammalian cis-PTase activity and function. SRD5A3-CDG affects the final step in dolichol synthesis. Its clinical features are typical for CDG type 1 glycosylation disorders including psychomotor retardation, ocular malformations, cerebellar hypoplasia, skin lesions, and facial dysmorphism
malfunction
-
the morphological differentiation of a Candida albicans cis-prenyltransferase mutant is impaired
-
metabolism
cis-Prenyltransferase is the first enzyme of the mevalonate pathway committed to the biosynthesis of dolichol in eukaryotes
metabolism
necessity of both dehydrodolichol diphosphate synthase, DHDDS or hCIT, and Nogo-B receptor, NgBR, for dolichol biosynthesis
metabolism
necessity of both dehydrodolichol diphosphate synthase, DHDDS or hCIT, and Nogo-B receptor, NgBR, for dolichol biosynthesis. Single subunit cis-PTases catalyze the condensation reactions of isopentenyl diphosphate (IPP) with farnesyl diphosphate (FPP) to synthesize linear polyprenyl diphosphate with specific chain lengths. Polyprenyl pyrophosphate is dephosphorylated into polyprenol and then reduced by a polyprenol reductase to produce dolichol
metabolism
-
cis-Prenyltransferase is the first enzyme of the mevalonate pathway committed to the biosynthesis of dolichol in eukaryotes
-
physiological function
-
dehydrodolichyl diphosphate synthase catalyzes the sequential condensation of isopentenyl diphosphate with farnesyl diphosphate to synthesize dehydrodolichyl diphosphate, a biosynthetic precursor for dolichol which plays an important role as a sugar-carrier lipid in the biosynthesis of glycoprotein in eukaryotic cells. Identification of a specific interaction of human dehydrodolichyl diphosphate synthase with the NiemannPick Type C2 protein (NPC2/HE1), whose defects cause NiemannPick type C2 disease
physiological function
involved in biosynthesis of dolichol (a long-chain polyprenol with a saturated alpha-isoprene unit, which serves as a glycosyl carrier in protein glycosylation). Of the two isozymes, Rer2p and Srt1p, isoenzyme Rer2p is responsible for the main activity of the wild-type cells, and the expression of RER2 is highest in the early logarithmic phase when the cells are actively dividing
physiological function
key enzyme in dolichol biosynthesis, the identity of the cloned enzyme is confirmed by functional complementation of a yeast mutant strain defective in dehydrodolichyl-diphosphates synthase activity, Arabidopsis thaliana enzyme catalyzes the synthesis of dehydrodolichyl-diphosphates with chain lengths similar to those found in yeast
physiological function
over-expression of SRT1 suppresses the growth and glycosylation defects of rer2. SRT1 has only a minor contribution to total cis-prenyltransferase activity under normal conditions
physiological function
RER2 encodes a key enzyme of dolichol synthesis
physiological function
cis-prenyltransferase is committed to the synthesis of dolichol, the Nogo-B receptor, NgBR, is a subunit required for dolichol synthesis in humans, essential role of NgBR in dolichol synthesis and protein glycosylation. NgBR as a protein interacts with reticulon 4B, also called Nogo-B
physiological function
cis-prenyltransferase is committed to the synthesis of dolichol, the Nogo-B receptor, NgBR, is a subunit required for dolichol synthesis in mice, essential role of NgBR in dolichol synthesis and protein glycosylation
physiological function
cis-prenyltransferase Rer2 is required for protein glycosylation, cell wall integrity and hypha formation. Dolichols are essential not only for protein glycosylation and cell wall integrity but also for growth and development of Candida albicans
physiological function
the SlCPT3 and SlCPTBP proteins interact to form a functional dolichol synthase
physiological function
-
cis-prenyltransferase Rer2 is required for protein glycosylation, cell wall integrity and hypha formation. Dolichols are essential not only for protein glycosylation and cell wall integrity but also for growth and development of Candida albicans
-
physiological function
-
the SlCPT3 and SlCPTBP proteins interact to form a functional dolichol synthase
-
Show AA Sequence and Transmembrane Helices (3232 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
-
product distributions is shifted to longer region to give the C65C70 as the main products
K109A
-
product distributions is shifted to longer region to give the C65C70 as the main products
L113A
-
product distributions is shifted to longer region to give the C65C70 as the main products
additional information
additional information
construction of the PMET3RER2/rer2D mutant strain JOS18, and of ura3D::imm434/ura3D::imm434 RER2/rer2D::hisG mutant strain JOS14, and of ura3D::imm434/ura3D::imm434 RER2/rer2D::hisG-URA3-hisG mutant strain JOS13
additional information
-
construction of the PMET3RER2/rer2D mutant strain JOS18, and of ura3D::imm434/ura3D::imm434 RER2/rer2D::hisG mutant strain JOS14, and of ura3D::imm434/ura3D::imm434 RER2/rer2D::hisG-URA3-hisG mutant strain JOS13
-
additional information
generation a triple deletion strain, nus1DELTA/rer2DELTA/srt1DELTA, expressing the homomeric cis-PTase from Giardia lamblia (GlcisPT), GlcisPT on a plasmid with a URA3 marker, to support growth, functional complementation by recombinant expression of active human and Schizosaccharomyces pombe enzymes
additional information
-
generation a triple deletion strain, nus1DELTA/rer2DELTA/srt1DELTA, expressing the homomeric cis-PTase from Giardia lamblia (GlcisPT), GlcisPT on a plasmid with a URA3 marker, to support growth, functional complementation by recombinant expression of active human and Schizosaccharomyces pombe enzymes
additional information
-
generation a triple deletion strain, nus1DELTA/rer2DELTA/srt1DELTA, expressing the homomeric cis-PTase from Giardia lamblia (GlcisPT), GlcisPT on a plasmid with a URA3 marker, to support growth, functional complementation by recombinant expression of active human and Schizosaccharomyces pombe enzymes
-
additional information
generation of RNAi-mediated knockdown of SlCPT3 expression in plants, SlCPT3 gene expression and also polyisoprenoid contents are reduced by approximately 60% and 40%, respectively. Although transgenic plantlets are recovered that exhibit a higher degree of SlCPT3 knockdown, they do snot survive to maturity. Interaction analysis in planta of SlCPT3 and SlCPTBP proteins by introducing C-terminally Myc-tagged SlCPT3 and FLAG-tagged SlCPTBP versions into Nicotiana benthamiana leaves in the endoplasmic reticulum lumeninal side
additional information
-
generation of RNAi-mediated knockdown of SlCPT3 expression in plants, SlCPT3 gene expression and also polyisoprenoid contents are reduced by approximately 60% and 40%, respectively. Although transgenic plantlets are recovered that exhibit a higher degree of SlCPT3 knockdown, they do snot survive to maturity. Interaction analysis in planta of SlCPT3 and SlCPTBP proteins by introducing C-terminally Myc-tagged SlCPT3 and FLAG-tagged SlCPTBP versions into Nicotiana benthamiana leaves in the endoplasmic reticulum lumeninal side
additional information
-
generation of RNAi-mediated knockdown of SlCPT3 expression in plants, SlCPT3 gene expression and also polyisoprenoid contents are reduced by approximately 60% and 40%, respectively. Although transgenic plantlets are recovered that exhibit a higher degree of SlCPT3 knockdown, they do snot survive to maturity. Interaction analysis in planta of SlCPT3 and SlCPTBP proteins by introducing C-terminally Myc-tagged SlCPT3 and FLAG-tagged SlCPTBP versions into Nicotiana benthamiana leaves in the endoplasmic reticulum lumeninal side
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
-
half-life: 46 min, half-life is prolonged by immobilization on silica beads to 156 min
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene is endogenously induced by gibberellin, its induction is independent of ethylene regulation
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kharel, Y.; Takahashi, S.; Yamashita, S.; Koyama T.
In vivo interaction between the human dehydrodolichyl diphosphate synthase and the Niemann-Pick C2 protein revealed by a yeast two-hybrid system
Biochem. Biophys. Res. Commun.
318
198-203
2004
Homo sapiens
brenda
Endo, S.; Zhang, Y.W.; Takahashi, S.; Koyama, T.
Identification of human dehydrodolichyl diphosphate synthase gene
Biochim. Biophys. Acta
1625
291-295
2003
Homo sapiens (Q86SQ9), Homo sapiens
brenda
Poznanski, J.; Szkopinska, A.
Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae
Biopolymers
86
155-164
2007
Saccharomyces cerevisiae (P35196), Saccharomyces cerevisiae (Q03175), Saccharomyces cerevisiae
brenda
Kurisaki, A.; Sagami, H.; Ogura, K.
Proteolytic release of dehydrodolichyl diphosphate synthase from pig testis microsomes
Biosci. Biotechnol. Biochem.
60
1109-1114
1996
Sus scrofa
brenda
Rebl, A.; Anders, E.; Wimmers, K.; Goldammer, T.
Characterization of dehydrodolichyl diphosphate synthase gene in rainbow trout (Oncorhynchus mykiss)
Comp. Biochem. Physiol. B Biochem. Mol. Biol.
152
260-265
2009
Oncorhynchus mykiss (B6ETP4), Oncorhynchus mykiss
brenda
Cunillera, N.
Arro, M.; Fores, O.; Manzano, D.; Ferrer, A.: Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis
FEBS Lett.
477
170-174
2000
Arabidopsis thaliana (O80458), Arabidopsis thaliana
brenda
Sato, M.; Fujisaki, S.; Sato, K.; Nishimura, Y.; Nakano, A.
Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis
Genes Cells
6
495-506
2001
Saccharomyces cerevisiae (C7GM47), Saccharomyces cerevisiae (P35196), Saccharomyces cerevisiae
brenda
Matsuoka, S.; Sagami, H.; Kurisaki, A.; Ogura, K.
Variable product specificity of microsomal dehydrodolichyl diphosphate synthase from rat liver
J. Biol. Chem.
266
3464-3468
1991
Rattus norvegicus
brenda
Oh, S.K.; Han, K.H.; Ryu, S.B.; Kang, H.
Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. Implications in rubber biosynthesis
J. Biol. Chem.
275
18482-18488
2000
Arabidopsis thaliana (O80458)
brenda
Yamada, Y.; Fukuda, W.; Hirooka, K.; Hiromoto, T.; Nakayama, J.; Imanaka, T.; Fukusaki, E.; Fujiwara, S.
Efficient in vitro synthesis of cis-polyisoprenes using a thermostable cis-prenyltransferase from a hyperthermophilic archaeon Thermococcus kodakaraensis
J. Biotechnol.
143
151-156
2009
Thermococcus kodakarensis
brenda
Sato, M.; Sato, K.; Nishikawa, S.; Hirata, A.; Kato, J.; Nakano, A.
The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis
Mol. Cell. Biol.
19
471-483
1999
Saccharomyces cerevisiae (C7GM47), Saccharomyces cerevisiae
brenda
Liu, M.C.; Wang, B.J.; Huang, J.K.; Wang, C.S.
Expression, localization and function of a cis-prenyltransferase in the tapetum and microspores of lily anthers
Plant Cell Physiol.
52
1487-1500
2011
Lilium longiflorum (B2BA86)
brenda
Park, E.J.; Grabinska, K.A.; Guan, Z.; Stranecky, V.; Hartmannova, H.; Hodanova, K.; Baresova, V.; Sovova, J.; Jozsef, L.; Ondruskova, N.; Hansikova, H.; Honzik, T.; Zeman, J.; Hulkova, H.; Wen, R.; Kmoch, S.; Sessa, W.C.
Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation
Cell Metab.
20
448-457
2014
Saccharomyces cerevisiae (Q12063), Saccharomyces cerevisiae, Homo sapiens (Q96E22), Homo sapiens, Mus musculus (Q99LJ8), Schizosaccharomyces pombe (Q9Y7K8), Saccharomyces cerevisiae BY4742 (Q12063)
brenda
Juchimiuk, M.; Orlowski, J.; Gawarecka, K.; Swiezewska, E.; Ernst, J.F.; Palamarczyk, G.
Candida albicans cis-prenyltransferase Rer2 is required for protein glycosylation, cell wall integrity and hypha formation
Fungal Genet. Biol.
69
1-12
2014
Candida albicans (Q5AJZ3), Candida albicans ATCC MYA-2876 (Q5AJZ3)
brenda
Brasher, M.I.; Surmacz, L.; Leong, B.; Pitcher, J.; Swiezewska, E.; Pichersky, E.; Akhtar, T.A.
A two-component enzyme complex is required for dolichol biosynthesis in tomato
Plant J.
82
903-914
2015
Solanum lycopersicum (K7WCI9), Solanum lycopersicum, Solanum lycopersicum MP-1 (K7WCI9)
brenda
Kwon, M.; Kwon, E.J.; Ro, D.K.
cis-Prenyltransferase and polymer analysis from a natural rubber perspective
Methods Enzymol.
576
121-145
2016
Saccharomyces cerevisiae, Arabidopsis thaliana (O80458)
brenda
Surowiecki, P.; Onysk, A.; Manko, K.; Swiezewska, E.; Surmacz, L.
Long-chain polyisoprenoids are synthesized by AtCPT1 in Arabidopsis thaliana
Molecules
24
2789
2019
Arabidopsis thaliana (O80458)
brenda
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