From Wikipedia, the free encyclopedia
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
⇌
{\displaystyle \rightleftharpoons }
n
diphosphate + ditrans, polycis-polyprenyl diphosphate (n
⇌
{\displaystyle \rightleftharpoons }
10--55)
The enzyme is involved in biosynthesis of
dolichol (a long-chain
polyprenol ) with a saturated alpha-isoprene unit.
References
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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 .
External links
Activity Regulation Classification Kinetics Types