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

Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)
Identifiers
EC number	2.5.1.87
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ n diphosphate + ditrans,polycis-polyprenyl diphosphate (n $\rightleftharpoons$ 10--55)

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. (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 83905. 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.

External links

• Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific) at the US National Library of Medicine Medical Subject Headings (MeSH)