Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups

malonyl-CoA:very-long-chain acyl-CoA malonyltransferase (decarboxylating and thioester-hydrolysing)

a very-long-chain acyl-CoA + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA [RN:R10825]

R10825;
(other) R07758 R07762 R09419

very-long-chain acyl-CoA [CPD:C20876];
malonyl-CoA [CPD:C00083]

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

EC 2.3.1.199 created 2012

1  [PMID:8702485]

Toke DA, Martin CE

Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae.

J Biol Chem 271:18413-22 (1996)
DOI:10.1074/jbc.271.31.18413

[sce:YJL196C]

2  [PMID:9211877]

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.

J Biol Chem 272:17376-84 (1997)
DOI:10.1074/jbc.272.28.17376

[sce:YCR034W YLR372W]

3  [PMID:9546663]

Dittrich F, Zajonc D, Huhne 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.

Eur J Biochem 252:477-85 (1998)
DOI:10.1046/j.1432-1327.1998.2520477.x

[sce:YJL196C]

4  [PMID:10330468]

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.

Plant Cell 11:825-38 (1999)

[ath:AT1G68530]

5  [PMID:12135493]

Ghanevati M, Jaworski JG

Engineering and mechanistic studies of the Arabidopsis FAE1 beta-ketoacyl-CoA synthase, FAE1 KCS.

Eur J Biochem 269:3531-9 (2002)
DOI:10.1046/j.1432-1033.2002.03039.x

6  [PMID:16765910]

Blacklock BJ, Jaworski JG

Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases.

Biochem Biophys Res Commun 346:583-90 (2006)
DOI:10.1016/j.bbrc.2006.05.162

[ath:AT1G01120 AT2G26640 AT4G34510]

7  [PMID:17719544]

Denic V, Weissman JS

A molecular caliper mechanism for determining very long-chain fatty acid length.

Cell 130:663-77 (2007)
DOI:10.1016/j.cell.2007.06.031

8  [PMID:22284369]

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 (2012)
DOI:10.1016/j.phytochem.2011.12.023