EC 2.3.1.199 - Very-long-chain 3-oxoacyl-CoA synthase

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IntEnz Enzyme Nomenclature
EC 2.3.1.199

Names

Accepted name:
very-long-chain 3-oxoacyl-CoA synthase
Other names:
very-long-chain 3-ketoacyl-CoA synthase
very-long-chain β-ketoacyl-CoA synthase
condensing enzyme [ambiguous]
CUT1 (gene name)
CER6 (gene name)
FAE1 (gene name)
KCS (gene name)
ELO (gene name)
Systematic name:
malonyl-CoA:very-long-chain acyl-CoA malonyltransferase (decarboxylating and thioester-hydrolysing)

Reaction

Comments:

This is the first component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. Multiple forms exist with differing preferences for the substrate, and thus the specific form expressed determines the local composition of very-long-chain fatty acids [6,7]. For example, the FAE1 form from the plant Arabidopsis thaliana accepts only 16 and 18 carbon substrates, with oleoyl-CoA (18:1) being the preferred substrate [5], while CER6 from the same plant prefers substrates with chain length of C22 to C32 [4,8]. cf. EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102336 , GO:0102337 , GO:0102338 , GO:0102756
UniProtKB/Swiss-Prot: (66) [show] [UniProt]

References

  1. Toke, D. A., Martin, C. E.
    Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae.
    J. Biol. Chem. 271: 18413-18422 (1996). [PMID: 8702485]
  2. Oh, C. S., Toke, D. A., Mandala, S., Martin, C. E.
    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: 17376-17384 (1997). [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.
    Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants.
    Eur. J. Biochem. 252: 477-485 (1998). [PMID: 9546663]
  4. Millar, A. A., Clemens, S., Zachgo, S., Giblin, E. M., Taylor, D. C., Kunst, L.
    CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme.
    Plant Cell 11: 825-838 (1999). [PMID: 10330468]
  5. Ghanevati, M., Jaworski, J. G.
    Engineering and mechanistic studies of the Arabidopsis FAE1 beta-ketoacyl-CoA synthase, FAE1 KCS.
    Eur. J. Biochem. 269: 3531-3539 (2002). [PMID: 12135493]
  6. Blacklock, B. J., Jaworski, J. G.
    Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases.
    Biochem. Biophys. Res. Commun. 346: 583-590 (2006). [PMID: 16765910]
  7. Denic, V., Weissman, J. S.
    A molecular caliper mechanism for determining very long-chain fatty acid length.
    Cell 130: 663-677 (2007). [PMID: 17719544]
  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: 162-171 (2012). [PMID: 22284369]

[EC 2.3.1.199 created 2012]