Biology:Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)
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| Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific) | |||||||||
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| 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] n diphosphate + ditrans, polycis-polyprenyl diphosphate (n [math]\displaystyle{ \rightleftharpoons }[/math] 10--55)
The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated alpha-isoprene unit.
References
- ↑ "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. June 2001. doi:10.1046/j.1365-2443.2001.00438.x. PMID 11442630.
- ↑ "Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae". Biopolymers 86 (2): 155–64. June 2007. doi:10.1002/bip.20715. PMID 17345630.
- ↑ "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. January 1999. doi:10.1128/mcb.19.1.471. PMID 9858571.
- ↑ "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. June 2000. doi:10.1074/jbc.M002000200. PMID 10764783.
- ↑ "Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis". FEBS Letters 477 (3): 170–4. July 2000. 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)
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