Very-long-chain 3-oxoacyl-CoA synthase

Very-long-chain 3-oxoacyl-CoA synthase
Identifiers
EC number	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
Search PMC articles PubMed articles NCBI proteins

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 (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-CoA $\rightleftharpoons$ 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.

References

1. Toke, D.A.; Martin, C.E. (1996). "Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae". J. Biol. Chem. 271 (31): 18413–18422. doi:10.1074/jbc.271.31.18413. PMID 8702485.
2. Oh, C.S.; Toke, D.A.; Mandala, S.; Martin, C.E. (1997). "ELO₂ and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation". J. Biol. Chem. 272 (28): 17376–17384. doi:10.1074/jbc.272.28.17376. PMID 9211877.
3. Dittrich, F.; Zajonc, D.; Huhne, K.; Hoja, U.; Ekici, A.; Greiner, E.; Klein, H.; Hofmann, J.; Bessoule, J.J.; Sperling, P.; Schweizer, E. (1998). "Fatty acid elongation in yeast⁻-biochemical characteristics of the enzyme system and isolation of elongation-defective mutants". Eur. J. Biochem. 252 (3): 477–485. doi:10.1046/j.1432-1327.1998.2520477.x. PMID 9546663.
4. Millar, A.A.; Clemens, S.; Zachgo, S.; Giblin, E.M.; Taylor, D.C.; Kunst, L. (1999). "CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme". Plant Cell. 11 (5): 825–838. doi:10.2307/3870817. PMID 10330468.
5. Ghanevati, M.; Jaworski, J.G. (2002). "Engineering and mechanistic studies of the Arabidopsis FAE1 β-ketoacyl-CoA synthase, FAE1 KCS". Eur. J. Biochem. 269 (14): 3531–3539. doi:10.1046/j.1432-1033.2002.03039.x. PMID 12135493.
6. Blacklock, B.J.; Jaworski, J.G. (2006). "Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases". Biochem. Biophys. Res. Commun. 346 (2): 583–590. doi:10.1016/j.bbrc.2006.05.162. PMID 16765910.
7. Denic, V.; Weissman, J.S. (2007). "A molecular caliper mechanism for determining very long-chain fatty acid length". Cell. 130 (4): 663–677. doi:10.1016/j.cell.2007.06.031. PMID 17719544.
8. Tresch, S.; Heilmann, M.; Christiansen, N.; Looser, R.; Grossmann, K. (2012). "Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases". Phytochemistry. 76: 162–171. doi:10.1016/j.phytochem.2011.12.023. PMID 22284369.

External links

• Very-long-chain 3-oxoacyl-CoA synthase at the US National Library of Medicine Medical Subject Headings (MeSH)