Biology:Very-long-chain 3-oxoacyl-CoA synthase
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Very-long-chain 3-oxoacyl-CoA synthase | |||||||||
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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 | ||||||||
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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
- ↑ "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.
- ↑ 2.0 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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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
- Very-long-chain+3-oxoacyl-CoA+synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/Very-long-chain 3-oxoacyl-CoA synthase.
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