Very-long-chain 3-oxoacyl-CoA synthase
(Redirected from ELO (gene))
| Very-long-chain 3-oxoacyl-CoA synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.199 | ||||||||
| 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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Very-long-chain 3-oxoacyl-CoA synthase (EC 2.3.1.199, very-long-chain 3-ketoacyl-CoA synthase, very-long-chain beta-ketoacyl-CoA synthase, condensing enzyme, CUT1, CER6, FAE1, KCS, ELO) is an enzyme with systematic name malonyl-CoA:very-long-chain acyl-CoA malonyltransferase (decarboxylating and thioester-hydrolysing).[1][2][3][4][5][6][7][8] This enzyme catalyses the following chemical reaction
- very-long-chain acyl-CoA + malonyl-CoA very-long-chain 3-oxoacyl-CoA + CO2 + coenzyme A
This is the first component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA to very-long-chain acyl CoAs. (Very-long-chain in this context refers, for example, to the C26 fatty acids involved in the synthesis of phospholipids and ceramides.[2]
References
[edit]- ^ Toke DA, Martin CE (August 1996). "Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae". The Journal of Biological Chemistry. 271 (31): 18413–22. doi:10.1074/jbc.271.31.18413. PMID 8702485.
- ^ a b Oh CS, Toke DA, Mandala S, Martin CE (July 1997). "ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation". The Journal of Biological Chemistry. 272 (28): 17376–84. doi:10.1074/jbc.272.28.17376. PMID 9211877.
- ^ Dittrich F, Zajonc D, Hühne K, Hoja U, Ekici A, Greiner E, Klein H, Hofmann J, Bessoule JJ, Sperling P, Schweizer E (March 1998). "Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants". European Journal of Biochemistry. 252 (3): 477–85. doi:10.1046/j.1432-1327.1998.2520477.x. PMID 9546663.
- ^ Millar AA, Clemens S, Zachgo S, Giblin EM, Taylor DC, Kunst L (May 1999). "CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme". The Plant Cell. 11 (5): 825–38. doi:10.2307/3870817. JSTOR 3870817. PMC 144219. PMID 10330468.
- ^ Ghanevati M, Jaworski JG (July 2002). "Engineering and mechanistic studies of the Arabidopsis FAE1 beta-ketoacyl-CoA synthase, FAE1 KCS". European Journal of Biochemistry. 269 (14): 3531–9. doi:10.1046/j.1432-1033.2002.03039.x. PMID 12135493.
- ^ Blacklock BJ, Jaworski JG (July 2006). "Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases". Biochemical and Biophysical Research Communications. 346 (2): 583–90. doi:10.1016/j.bbrc.2006.05.162. PMID 16765910.
- ^ Denic V, Weissman JS (August 2007). "A molecular caliper mechanism for determining very long-chain fatty acid length". Cell. 130 (4): 663–77. doi:10.1016/j.cell.2007.06.031. PMID 17719544.
- ^ Tresch S, Heilmann M, Christiansen N, Looser R, Grossmann K (April 2012). "Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases". Phytochemistry. 76: 162–71. Bibcode:2012PChem..76..162T. doi:10.1016/j.phytochem.2011.12.023. PMID 22284369.
External links
[edit]- Very-long-chain+3-oxoacyl-CoA+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
