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

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Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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

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


  1. ^ Sato, M.; Fujisaki, S.; Sato, K.; Nishimura, Y.; Nakano, A. (2001). "Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis". Genes Cells. 6 (6): 495–506. doi:10.1046/j.1365-2443.2001.00438.x. PMID 11442630. 
  2. ^ Poznanski, J.; Szkopinska, A. (2007). "Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae". Biopolymers. 86 (2): 155–164. doi:10.1002/bip.20715. PMID 17345630. 
  3. ^ Sato, M.; Sato, K.; Nishikawa, S.; Hirata, A.; Kato, J.; Nakano, A. (1999). "The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis". Mol. Cell. Biol. 19 (1): 471–483. doi:10.1128/mcb.19.1.471. PMC 83905Freely accessible. PMID 9858571. 
  4. ^ Oh, S.K.; Han, K.H.; Ryu, S.B.; Kang, H. (2000). "Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. Implications in rubber biosynthesis". J. Biol. Chem. 275 (24): 18482–18488. doi:10.1074/jbc.M002000200. PMID 10764783. 
  5. ^ Cunillera, N.; Arro, M.; Fores, O.; Manzano, D.; Ferrer, A. (2000). "Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis". FEBS Lett. 477 (3): 170–174. doi:10.1016/S0014-5793(00)01798-1. PMID 10908715. 

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