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Information on EC 2.5.1.87 - ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] and Organism(s) Homo sapiens and UniProt Accession Q86SQ9

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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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Homo sapiens
UNIPROT: Q86SQ9
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The taxonomic range for the selected organisms is: Homo sapiens
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
Dedol-PP synthase
-
dehydrodolichyl diphosphate synthase
-
cis-prenyltransferase
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cis-PTase
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DedolPP synthase
-
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dehydrodolichyl diphosphate synthase
-
-
Nogo-B receptor
-
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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expresses dehydrodolichyl diphosphate synthase mRNA at high levels
Manually annotated by BRENDA team
expresses dehydrodolichyl diphosphate synthase mRNA at high levels
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
enzyme NgBR is a polytypic membrane protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
amino acid at 4th position from the C-terminus of NgBR is a functionally and evolutionary conserved residue
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
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
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHDDS_HUMAN
333
0
38657
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression the gene in a yeast mutant strain SNH23-7D
functional expression in Saccaromyces cerevisiae nus1DELTA/rer2DELTA/srt1DELTA mutant strain
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team