Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.5.1.87 - ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] and Organism(s) Mus musculus and UniProt Accession Q99LJ8

for references in articles please use BRENDA:EC2.5.1.87
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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) .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: Q99LJ8
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Mus musculus
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
-
cis-PTase
-
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
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
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
metabolism
necessity of both dehydrodolichol diphosphate synthase, DHDDS or hCIT, and Nogo-B receptor, NgBR, for dolichol biosynthesis
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NGBR_MOUSE
297
0
33485
Swiss-Prot
Secretory Pathway (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
generation of NgBR knockout mice
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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