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| Name = Very-long-chain 3-oxoacyl-CoA synthase
| EC_number = 2.3.1.199
| CAS_number =
| IUBMB_EC_number = 2/3/1/199
| GO_code =
| image =
| width =
| caption =
}}Very-long-chain 3-oxoacyl-CoA synthase ({{EC number|2.3.1.199}}, very-long-chain 3-ketoacyl-CoA synthase, very-long-chain beta-ketoacyl-CoA synthase, condensing enzyme, CUT1 (gene), CER6 (gene), FAE1 (gene), KCS (gene), ELO (gene)) 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-CoAvery-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.
References
1. ^{{cite journal | vauthors = Toke DA, Martin CE | title = Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae | journal = The Journal of Biological Chemistry | volume = 271 | issue = 31 | pages = 18413–22 | date = August 1996 | pmid = 8702485 | doi = 10.1074/jbc.271.31.18413 }}
2. ^{{cite journal | vauthors = Oh CS, Toke DA, Mandala S, Martin CE | title = ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation | journal = The Journal of Biological Chemistry | volume = 272 | issue = 28 | pages = 17376–84 | date = July 1997 | pmid = 9211877 | doi = 10.1074/jbc.272.28.17376 }}
3. ^{{cite journal | vauthors = Dittrich F, Zajonc D, Hühne K, Hoja U, Ekici A, Greiner E, Klein H, Hofmann J, Bessoule JJ, Sperling P, Schweizer E | title = Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants | journal = European Journal of Biochemistry | volume = 252 | issue = 3 | pages = 477–85 | date = March 1998 | pmid = 9546663 | doi = 10.1046/j.1432-1327.1998.2520477.x }}
4. ^{{cite journal | vauthors = Millar AA, Clemens S, Zachgo S, Giblin EM, Taylor DC, Kunst L | title = CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme | journal = The Plant Cell | volume = 11 | issue = 5 | pages = 825–38 | date = May 1999 | pmid = 10330468 | pmc = 144219 | doi = 10.2307/3870817 }}
5. ^{{cite journal | vauthors = Ghanevati M, Jaworski JG | title = Engineering and mechanistic studies of the Arabidopsis FAE1 beta-ketoacyl-CoA synthase, FAE1 KCS | journal = European Journal of Biochemistry | volume = 269 | issue = 14 | pages = 3531–9 | date = July 2002 | pmid = 12135493 | doi = 10.1046/j.1432-1033.2002.03039.x }}
6. ^{{cite journal | vauthors = Blacklock BJ, Jaworski JG | title = Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases | journal = Biochemical and Biophysical Research Communications | volume = 346 | issue = 2 | pages = 583–90 | date = July 2006 | pmid = 16765910 | doi = 10.1016/j.bbrc.2006.05.162 }}
7. ^{{cite journal | vauthors = Denic V, Weissman JS | title = A molecular caliper mechanism for determining very long-chain fatty acid length | journal = Cell | volume = 130 | issue = 4 | pages = 663–77 | date = August 2007 | pmid = 17719544 | doi = 10.1016/j.cell.2007.06.031 }}
8. ^{{cite journal | vauthors = Tresch S, Heilmann M, Christiansen N, Looser R, Grossmann K | title = Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases | journal = Phytochemistry | volume = 76 | pages = 162–71 | date = April 2012 | pmid = 22284369 | doi = 10.1016/j.phytochem.2011.12.023 }}
2. ^{{cite journal | vauthors = Oh CS, Toke DA, Mandala S, Martin CE | title = ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation | journal = The Journal of Biological Chemistry | volume = 272 | issue = 28 | pages = 17376–84 | date = July 1997 | pmid = 9211877 | doi = 10.1074/jbc.272.28.17376 }}
3. ^{{cite journal | vauthors = Dittrich F, Zajonc D, Hühne K, Hoja U, Ekici A, Greiner E, Klein H, Hofmann J, Bessoule JJ, Sperling P, Schweizer E | title = Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants | journal = European Journal of Biochemistry | volume = 252 | issue = 3 | pages = 477–85 | date = March 1998 | pmid = 9546663 | doi = 10.1046/j.1432-1327.1998.2520477.x }}
4. ^{{cite journal | vauthors = Millar AA, Clemens S, Zachgo S, Giblin EM, Taylor DC, Kunst L | title = CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme | journal = The Plant Cell | volume = 11 | issue = 5 | pages = 825–38 | date = May 1999 | pmid = 10330468 | pmc = 144219 | doi = 10.2307/3870817 }}
5. ^{{cite journal | vauthors = Ghanevati M, Jaworski JG | title = Engineering and mechanistic studies of the Arabidopsis FAE1 beta-ketoacyl-CoA synthase, FAE1 KCS | journal = European Journal of Biochemistry | volume = 269 | issue = 14 | pages = 3531–9 | date = July 2002 | pmid = 12135493 | doi = 10.1046/j.1432-1033.2002.03039.x }}
6. ^{{cite journal | vauthors = Blacklock BJ, Jaworski JG | title = Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases | journal = Biochemical and Biophysical Research Communications | volume = 346 | issue = 2 | pages = 583–90 | date = July 2006 | pmid = 16765910 | doi = 10.1016/j.bbrc.2006.05.162 }}
7. ^{{cite journal | vauthors = Denic V, Weissman JS | title = A molecular caliper mechanism for determining very long-chain fatty acid length | journal = Cell | volume = 130 | issue = 4 | pages = 663–77 | date = August 2007 | pmid = 17719544 | doi = 10.1016/j.cell.2007.06.031 }}
8. ^{{cite journal | vauthors = Tresch S, Heilmann M, Christiansen N, Looser R, Grossmann K | title = Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases | journal = Phytochemistry | volume = 76 | pages = 162–71 | date = April 2012 | pmid = 22284369 | doi = 10.1016/j.phytochem.2011.12.023 }}
External links
- {{MeshName|Very-long-chain+3-oxoacyl-CoA+synthase}}
1 : EC 2.3.1
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