Biology:Very-long-chain 3-oxoacyl-CoA synthase

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Very-long-chain 3-oxoacyl-CoA synthase
Identifiers
EC number2.3.1.199
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 [math]\displaystyle{ \rightleftharpoons }[/math] 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. (Very-long-chain in this context refers, for example, to the C26 fatty acids involved in the synthesis of phospholipids and ceramides.[2]

References

  1. "Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae". The Journal of Biological Chemistry 271 (31): 18413–22. August 1996. doi:10.1074/jbc.271.31.18413. PMID 8702485. 
  2. 2.0 2.1 "ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation". The Journal of Biological Chemistry 272 (28): 17376–84. July 1997. doi:10.1074/jbc.272.28.17376. PMID 9211877. 
  3. "Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants". European Journal of Biochemistry 252 (3): 477–85. March 1998. doi:10.1046/j.1432-1327.1998.2520477.x. PMID 9546663. 
  4. "CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme". The Plant Cell 11 (5): 825–38. May 1999. doi:10.2307/3870817. PMID 10330468. 
  5. "Engineering and mechanistic studies of the Arabidopsis FAE1 beta-ketoacyl-CoA synthase, FAE1 KCS". European Journal of Biochemistry 269 (14): 3531–9. July 2002. doi:10.1046/j.1432-1033.2002.03039.x. PMID 12135493. 
  6. "Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases". Biochemical and Biophysical Research Communications 346 (2): 583–90. July 2006. doi:10.1016/j.bbrc.2006.05.162. PMID 16765910. 
  7. "A molecular caliper mechanism for determining very long-chain fatty acid length". Cell 130 (4): 663–77. August 2007. doi:10.1016/j.cell.2007.06.031. PMID 17719544. 
  8. "Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases". Phytochemistry 76: 162–71. April 2012. doi:10.1016/j.phytochem.2011.12.023. PMID 22284369. 

External links