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

Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific) (EC 2.5.1.87, RER2, Rer2p, Rer2p Z-prenyltransferase, Srt1p, Srt2p Z-prenyltransferase, ACPT, dehydrodolichyl diphosphate synthase 1) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 10--55 isopentenyl units).[1][2][3][4][5] This enzyme catalyses the following chemical reaction

(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate n diphosphate + ditrans, polycis-polyprenyl diphosphate (n 10--55)
Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)
Identifiers
EC number2.5.1.87
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated alpha-isoprene unit.

References
  1. Sato M, Fujisaki S, Sato K, Nishimura Y, Nakano A (June 2001). "Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis". Genes to Cells. 6 (6): 495–506. doi:10.1046/j.1365-2443.2001.00438.x. PMID 11442630.
  2. Poznański J, Szkopinska A (June 2007). "Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae". Biopolymers. 86 (2): 155–64. doi:10.1002/bip.20715. PMID 17345630.
  3. Sato M, Sato K, Nishikawa S, Hirata A, Kato J, Nakano A (January 1999). "The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis". Molecular and Cellular Biology. 19 (1): 471–83. doi:10.1128/mcb.19.1.471. PMC 83905. PMID 9858571.
  4. Oh SK, Han KH, Ryu SB, Kang H (June 2000). "Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. Implications in rubber biosynthesis". The Journal of Biological Chemistry. 275 (24): 18482–8. doi:10.1074/jbc.M002000200. PMID 10764783.
  5. Cunillera N, Arró M, Forés O, Manzano D, Ferrer A (July 2000). "Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis". FEBS Letters. 477 (3): 170–4. doi:10.1016/S0014-5793(00)01798-1. PMID 10908715.
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