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Information on EC 2.5.1.87 - ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] and Organism(s) Arabidopsis thaliana and UniProt Accession O80458

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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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Arabidopsis thaliana
UNIPROT: O80458
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
dhdds, nogo-b receptor, rer2p, tk-idsb, srt1p, slcpt3, dedol-pp synthase, cis-ptase, dedolpp synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cis-prenyltransferase
-
Dedol-PP synthase
-
dehydrodolichyl diphosphate synthase 1
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 10–55 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].
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 + 21 isopentenyl diphosphate
21 diphosphate + di-trans,poly-cis tetracosaprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + dehydrodolichyl diphosphate
show the reaction diagram
-
-
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
show the reaction diagram
-
-
-
-
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
-
?
additional information
?
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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
(2E,6E)-farnesyl diphosphate + 21 isopentenyl diphosphate
21 diphosphate + di-trans,poly-cis tetracosaprenyl diphosphate
show the reaction diagram
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 + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
show the reaction diagram
-
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
(2E,6E)-farnesyl diphosphate
pH 7.5, 30°C
0.00362
geranylgeranyl diphosphate
pH 7.5, 30°C
0.023
isopentenyl diphosphate
pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.05
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DDPS1_ARATH
303
1
34975
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
x * 33000, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 33000, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana benthamiana leaves
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
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team