IUBMB Enzyme Nomenclature


Accepted name: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]

Reaction: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10-55)

For diagram of reaction, click here

Other name(s): RER2; Rer2p; Rer2p Z-prenyltransferase; Srt1p; Srt2p Z-prenyltransferase; ACPT; dehydrodolichyl diphosphate synthase 1

Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 10-55 isopentenyl units)

Comments: The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol with a saturated α-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 C80 (16 isoprene residues) extending to C120, while Srt1p synthesizes mainly polyprenol with 22 isoprene subunits. Largest Srt1p products reach C290 [2]. The enzyme from Arabidopsis thaliana catalyses the formation of polyprenyl diphosphates with predominant carbon number C120 [4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:


1. Sato, M., Fujisaki, S., Sato, K., Nishimura, Y. and Nakano, A. Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6 (2001) 495-506. [PMID: 11442630]

2. Poznanski, J. and Szkopinska, A. Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae. Biopolymers 86 (2007) 155-164. [PMID: 17345630]

3. Sato, M., Sato, K., Nishikawa, S., Hirata, A., Kato, J. and Nakano, A. The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol. Cell Biol. 19 (1999) 471-483. [PMID: 9858571]

4. Oh, S.K., Han, K.H., Ryu, S.B. and Kang, H. Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. Implications in rubber biosynthesis. J. Biol. Chem. 275 (2000) 18482-18488. [PMID: 10764783]

5. Cunillera, N., Arro, M., Fores, O., Manzano, D. and Ferrer, A. Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis. FEBS Lett. 477 (2000) 170-174. [PMID: 10908715]

[EC created 2010]

Return to EC 2.5.1 home page
Return to EC 2.5 home page
Return to EC 2 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page