View source for Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)

{{Infobox enzyme
| Name       = Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)
| EC_number  = 2.5.1.87
| CAS_number =
| GO_code    =
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'''Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)''' ({{EC number|2.5.1.87}}, ''RER2'', ''Rer2p'', ''Rer2p Z-prenyltransferase'', ''Srt1p'', ''Srt2p Z-prenyltransferase'', ''ACPT'', ''dehydrodolichyl diphosphate synthase 1'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''(2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 10--55 isopentenyl units)''.<ref>{{cite journal | vauthors = Sato M, Fujisaki S, Sato K, Nishimura Y, Nakano A | title = Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis | journal = Genes to Cells | volume = 6 | issue = 6 | pages = 495–506 | date = June 2001 | pmid = 11442630 | doi = 10.1046/j.1365-2443.2001.00438.x | doi-access = free }}</ref><ref>{{cite journal | vauthors = Poznański J, Szkopinska A | title = Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae | journal = Biopolymers | volume = 86 | issue = 2 | pages = 155–64 | date = June 2007 | pmid = 17345630 | doi = 10.1002/bip.20715 }}</ref><ref>{{cite journal | vauthors = Sato M, Sato K, Nishikawa S, Hirata A, Kato J, Nakano A | title = The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis | journal = Molecular and Cellular Biology | volume = 19 | issue = 1 | pages = 471–83 | date = January 1999 | pmid = 9858571 | pmc = 83905 | doi = 10.1128/mcb.19.1.471 }}</ref><ref>{{cite journal | vauthors = Oh SK, Han KH, Ryu SB, Kang H | title = Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. Implications in rubber biosynthesis | journal = The Journal of Biological Chemistry | volume = 275 | issue = 24 | pages = 18482–8 | date = June 2000 | pmid = 10764783 | doi = 10.1074/jbc.M002000200 | doi-access =free  }}</ref><ref>{{cite journal | vauthors = Cunillera N, Arró M, Forés O, Manzano D, Ferrer A | title = Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis | journal = FEBS Letters | volume = 477 | issue = 3 | pages = 170–4 | date = July 2000 | pmid = 10908715 | doi = 10.1016/S0014-5793(00)01798-1 | doi-access =  }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
: (2E,6E)-farnesyl diphosphate + n [[isopentenyl diphosphate]] <math>\rightleftharpoons</math> n [[diphosphate]] + ditrans, polycis-polyprenyl diphosphate (n <math>\rightleftharpoons</math> 10--55)
The enzyme is involved in biosynthesis of [[dolichol]] (a long-chain [[polyprenol]]) with a saturated alpha-isoprene unit.
== References ==
{{reflist}}
== External links ==
* {{MeshName|Ditrans,polycis-polyprenyl+diphosphate+synthase+((2E,6E)-farnesyl+diphosphate+specific)}}
{{Alkyl and aryl transferases}}
{{Enzymes}}
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[[Category:EC 2.5.1]]