Very-long-chain 3-oxoacyl-CoA synthase
| 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 | ||||||||
| |||||||||
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 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
- ^ Toke, D.A. and 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - ^ Oh, C.S., Toke, D.A., Mandala, S. and 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - ^ Dittrich, F., Zajonc, D., Huhne, K., Hoja, U., Ekici, A., Greiner, E., Klein, H., Hofmann, J., Bessoule, J.J., Sperling, P. and 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Millar, A.A., Clemens, S., Zachgo, S., Giblin, E.M., Taylor, D.C. and 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Ghanevati, M. and 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Blacklock, B.J. and 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Denic, V. and 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Tresch, S., Heilmann, M., Christiansen, N., Looser, R. and 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- Very-long-chain+3-oxoacyl-CoA+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)