Very-long-chain 3-oxoacyl-CoA synthase explained

Very-long-chain 3-oxoacyl-CoA synthase
Ec Number:	2.3.1.199

Very-long-chain 3-oxoacyl-CoA synthase (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

\rightleftharpoons 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.

Notes and References

1. Toke DA, Martin CE . Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae . The Journal of Biological Chemistry . 271 . 31 . 18413–22 . August 1996 . 8702485 . 10.1074/jbc.271.31.18413 . free .
2. Oh CS, Toke DA, Mandala S, Martin CE . 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 . July 1997 . 9211877 . 10.1074/jbc.272.28.17376 . free .
3. Dittrich F, Zajonc D, Hühne K, Hoja U, Ekici A, Greiner E, Klein H, Hofmann J, Bessoule JJ, Sperling P, Schweizer E . 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 . March 1998 . 9546663 . 10.1046/j.1432-1327.1998.2520477.x . free .
4. Millar AA, Clemens S, Zachgo S, Giblin EM, Taylor DC, Kunst L . 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 . May 1999 . 10330468 . 144219 . 10.2307/3870817 . 3870817 .
5. Ghanevati M, Jaworski JG . Engineering and mechanistic studies of the Arabidopsis FAE1 beta-ketoacyl-CoA synthase, FAE1 KCS . European Journal of Biochemistry . 269 . 14 . 3531–9 . July 2002 . 12135493 . 10.1046/j.1432-1033.2002.03039.x .
6. Blacklock BJ, Jaworski JG . Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases . Biochemical and Biophysical Research Communications . 346 . 2 . 583–90 . July 2006 . 16765910 . 10.1016/j.bbrc.2006.05.162 .
7. Denic V, Weissman JS . A molecular caliper mechanism for determining very long-chain fatty acid length . Cell . 130 . 4 . 663–77 . August 2007 . 17719544 . 10.1016/j.cell.2007.06.031 . free .
8. Tresch S, Heilmann M, Christiansen N, Looser R, Grossmann K . Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases . Phytochemistry . 76 . 162–71 . April 2012 . 22284369 . 10.1016/j.phytochem.2011.12.023 . 2012PChem..76..162T .