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Record Information
StatusExpected but not Quantified
Creation Date2005-11-16 15:48:42 UTC
Update Date2020-07-09 22:12:09 UTC
Secondary Accession Numbers
  • HMDB0060170
  • HMDB01064
  • HMDB60170
Metabolite Identification
Common NameLinoleoyl-CoA
DescriptionLinoleoyl-CoA is the acyl-CoA of linoleic acid found in the human body. It binds to and results in decreased activity of glutathione S-transferase1. It has been proposed that inhibition of mitochondrial adenine nucleotide translocator by long-chain acyl-CoA underlies the mechanism associating obesity and type 2 diabetes. Unsaturated fatty acids play an important role in the prevention of human diseases such as diabetes, obesity, cancer, and neurodegeneration. Their oxidation in vivo by acyl-CoA dehydrogenases (ACADs) catalyze the first step of each cycle of mitochondrial fatty acid beta-oxidation. ACAD-9 had maximal activity with long-chain unsaturated acyl-CoAs as substrates (PMID: 17184976 , 16020546 ).
Linoleoyl-coenzyme AHMDB
Linoleoyl-coenzyme A, (Z,Z)-isomerHMDB
Linoleic coenzyme AHMDB
Linoleoyl coenzyme AHMDB
Linoleyl-coenzyme AHMDB
(9Z,12Z)-Octadecadienoyl-coenzyme AHMDB
Chemical FormulaC39H66N7O17P3S
Average Molecular Weight1029.97
Monoisotopic Molecular Weight1029.344875861
IUPAC Name{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-2-({[hydroxy({hydroxy[(3R)-3-hydroxy-2,2-dimethyl-3-{[2-({2-[(9Z,12Z)-octadeca-9,12-dienoylsulfanyl]ethyl}carbamoyl)ethyl]carbamoyl}propoxy]phosphoryl}oxy)phosphoryl]oxy}methyl)oxolan-3-yl]oxy}phosphonic acid
Traditional Namelinoleoyl-coa
CAS Registry Number6709-57-5
InChI Identifier
Chemical Taxonomy
Description belongs to the class of organic compounds known as long-chain fatty acyl coas. These are acyl CoAs where the group acylated to the coenzyme A moiety is a long aliphatic chain of 13 to 21 carbon atoms.
KingdomOrganic compounds
Super ClassLipids and lipid-like molecules
ClassFatty Acyls
Sub ClassFatty acyl thioesters
Direct ParentLong-chain fatty acyl CoAs
Alternative Parents
  • Coenzyme a or derivatives
  • Purine ribonucleoside 3',5'-bisphosphate
  • Purine ribonucleoside bisphosphate
  • Purine ribonucleoside diphosphate
  • Ribonucleoside 3'-phosphate
  • Pentose phosphate
  • Pentose-5-phosphate
  • Beta amino acid or derivatives
  • Glycosyl compound
  • N-glycosyl compound
  • 6-aminopurine
  • Monosaccharide phosphate
  • Organic pyrophosphate
  • Pentose monosaccharide
  • Imidazopyrimidine
  • Purine
  • Monoalkyl phosphate
  • Aminopyrimidine
  • Imidolactam
  • N-acyl-amine
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Monosaccharide
  • Pyrimidine
  • Alkyl phosphate
  • Fatty amide
  • Phosphoric acid ester
  • Tetrahydrofuran
  • Imidazole
  • Azole
  • Heteroaromatic compound
  • Carbothioic s-ester
  • Secondary alcohol
  • Thiocarboxylic acid ester
  • Carboxamide group
  • Secondary carboxylic acid amide
  • Amino acid or derivatives
  • Sulfenyl compound
  • Thiocarboxylic acid or derivatives
  • Organoheterocyclic compound
  • Azacycle
  • Oxacycle
  • Carboxylic acid derivative
  • Organosulfur compound
  • Organic oxygen compound
  • Hydrocarbon derivative
  • Carbonyl group
  • Organic nitrogen compound
  • Primary amine
  • Organopnictogen compound
  • Organic oxide
  • Organooxygen compound
  • Organonitrogen compound
  • Alcohol
  • Amine
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors

Route of exposure:


Biological location:


Naturally occurring process:


Biological role:

Industrial application:

Physical Properties
Experimental Properties
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
Water Solubility0.86 g/LALOGPS
pKa (Strongest Acidic)0.82ChemAxon
pKa (Strongest Basic)4.01ChemAxon
Physiological Charge-4ChemAxon
Hydrogen Acceptor Count17ChemAxon
Hydrogen Donor Count9ChemAxon
Polar Surface Area363.63 ŲChemAxon
Rotatable Bond Count34ChemAxon
Refractivity248.08 m³·mol⁻¹ChemAxon
Polarizability103.13 ųChemAxon
Number of Rings3ChemAxon
Rule of FiveNoChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleYesChemAxon
Spectrum TypeDescriptionSplash KeyView
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 123V, negativesplash10-056r-1100903000-97979bc4426e696ca500Spectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 133V, negativesplash10-0a6r-2211903000-4df18afe923088dccc9dSpectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 135V, negativesplash10-0a6r-2311904000-084368125746db9a1a8dSpectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 160V, negativesplash10-056r-9834804000-ca985ff7e3a0a2cf068cSpectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 168V, negativesplash10-056r-9723402000-1ea9fba94f19b641305dSpectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 185V, negativesplash10-056r-9622100000-4bcd035304dec49a3addSpectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 199V, negativesplash10-004i-9511000000-1f5c4a5c6b6d8b944e54Spectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 218V, negativesplash10-004i-9410000000-cdcfa205f52edfcda7f1Spectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 232V, negativesplash10-004i-9400000000-678749dd033055882657Spectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 253V, negativesplash10-004i-9400000000-dcd823851fb7d4ad77a7Spectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 273V, negativesplash10-004i-9300000000-2e76dfce41f4d4f8fea5Spectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 304V, negativesplash10-004i-9300000000-6a4626bbeafb9da35d70Spectrum
LC-MS/MSLC-MS/MS Spectrum - n/a 72V, negativesplash10-001i-1000209003-f68430866c04428bfb90Spectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 47V, positivesplash10-001i-9000200000-2cabae93047abe4a748dSpectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 65V, positivesplash10-00fr-3000970000-f399f99de6048f888713Spectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 100V, positivesplash10-00di-0100590000-9dc110d2f0daecf49e4dSpectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 133V, positivesplash10-00dr-1930160000-1caa8491ab78bfd3d5a9Spectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 168V, positivesplash10-000i-2920000000-c8b0b7ed0a3db1633f65Spectrum
LC-MS/MSLC-MS/MS Spectrum - Orbitrap 247V, positivesplash10-000i-4900000000-70e58b576b80fd6196afSpectrum
LC-MS/MSLC-MS/MS Spectrum - n/a 72V, positivesplash10-00di-0000490000-7f3332450575be86b2d1Spectrum
Biological Properties
Cellular Locations
  • Extracellular
  • Membrane
Biospecimen LocationsNot Available
Tissue LocationsNot Available
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDNot Available
KNApSAcK IDNot Available
Chemspider ID4593690
KEGG Compound IDC02050
BioCyc IDCPD-18
BiGG IDNot Available
Wikipedia LinkNot Available
METLIN IDNot Available
PubChem Compound5497112
PDB IDNot Available
ChEBI ID15530
Food Biomarker OntologyNot Available
MarkerDB ID
Synthesis ReferenceKawaguchi, Akihiko; Yoshimura, Tsutomu; Okuda, Shigenobu. A new method for the preparation of acyl-CoA thioesters. Journal of Biochemistry (Tokyo, Japan) (1981), 89(2), 337-9.
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Ramsay RR, Mancinelli G, Arduini A: Carnitine palmitoyltransferase in human erythrocyte membrane. Properties and malonyl-CoA sensitivity. Biochem J. 1991 May 1;275 ( Pt 3):685-8. [PubMed:2039446 ]
  2. Domergue F, Abbadi A, Ott C, Zank TK, Zahringer U, Heinz E: Acyl carriers used as substrates by the desaturases and elongases involved in very long-chain polyunsaturated fatty acids biosynthesis reconstituted in yeast. J Biol Chem. 2003 Sep 12;278(37):35115-26. Epub 2003 Jun 30. [PubMed:12835316 ]
  3. Kawasaki T, Snyder F: Synthesis of a novel acetylated neutral lipid related to platelet-activating factor by acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol acyltransferase in HL-60 cells. J Biol Chem. 1988 Feb 25;263(6):2593-6. [PubMed:3422635 ]
  4. Thiele I, Swainston N, Fleming RM, Hoppe A, Sahoo S, Aurich MK, Haraldsdottir H, Mo ML, Rolfsson O, Stobbe MD, Thorleifsson SG, Agren R, Bolling C, Bordel S, Chavali AK, Dobson P, Dunn WB, Endler L, Hala D, Hucka M, Hull D, Jameson D, Jamshidi N, Jonsson JJ, Juty N, Keating S, Nookaew I, Le Novere N, Malys N, Mazein A, Papin JA, Price ND, Selkov E Sr, Sigurdsson MI, Simeonidis E, Sonnenschein N, Smallbone K, Sorokin A, van Beek JH, Weichart D, Goryanin I, Nielsen J, Westerhoff HV, Kell DB, Mendes P, Palsson BO: A community-driven global reconstruction of human metabolism. Nat Biotechnol. 2013 May;31(5):419-25. doi: 10.1038/nbt.2488. Epub 2013 Mar 3. [PubMed:23455439 ]
  5. Ciapaite J, Bakker SJ, Van Eikenhorst G, Wagner MJ, Teerlink T, Schalkwijk CG, Fodor M, Ouwens DM, Diamant M, Heine RJ, Westerhoff HV, Krab K: Functioning of oxidative phosphorylation in liver mitochondria of high-fat diet fed rats. Biochim Biophys Acta. 2007 Mar;1772(3):307-16. Epub 2006 Nov 10. [PubMed:17184976 ]
  6. Ensenauer R, He M, Willard JM, Goetzman ES, Corydon TJ, Vandahl BB, Mohsen AW, Isaya G, Vockley J: Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids. J Biol Chem. 2005 Sep 16;280(37):32309-16. Epub 2005 Jul 14. [PubMed:16020546 ]
  7. Simons K, Toomre D: Lipid rafts and signal transduction. Nat Rev Mol Cell Biol. 2000 Oct;1(1):31-9. [PubMed:11413487 ]
  8. Watson AD: Thematic review series: systems biology approaches to metabolic and cardiovascular disorders. Lipidomics: a global approach to lipid analysis in biological systems. J Lipid Res. 2006 Oct;47(10):2101-11. Epub 2006 Aug 10. [PubMed:16902246 ]
  9. Sethi JK, Vidal-Puig AJ: Thematic review series: adipocyte biology. Adipose tissue function and plasticity orchestrate nutritional adaptation. J Lipid Res. 2007 Jun;48(6):1253-62. Epub 2007 Mar 20. [PubMed:17374880 ]
  10. Lingwood D, Simons K: Lipid rafts as a membrane-organizing principle. Science. 2010 Jan 1;327(5961):46-50. doi: 10.1126/science.1174621. [PubMed:20044567 ]
  11. (). Silva C, Loyola G, Valenzuela R, García-Huidobro T, Monasterio O, Bronfman M. High-affinity binding of fatty acyl-CoAs and peroxisome proliferator-CoA esters to glutathione S-transferases effect on enzymatic activity. Eur J Biochem. 1999 Nov;266(1):143-50.. .
  12. Gunstone, Frank D., John L. Harwood, and Albert J. Dijkstra (2007). The lipid handbook with CD-ROM. CRC Press.


General function:
Involved in thiolester hydrolase activity
Specific function:
Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Lipid transport and metabolism
Specific function:
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA.
Gene Name:
Uniprot ID:
Molecular weight:
Linoleoyl-CoA + Water → Coenzyme A + Linoleic aciddetails
General function:
Involved in thiolester hydrolase activity
Specific function:
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs.
Gene Name:
Uniprot ID:
Molecular weight:
Linoleoyl-CoA + Water → Coenzyme A + Linoleic aciddetails
General function:
Involved in thiolester hydrolase activity
Specific function:
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (By similarity). Succinyl-CoA thioesterase that also hydrolyzes long chain saturated and unsaturated monocarboxylic acyl-CoAs.
Gene Name:
Uniprot ID:
Molecular weight:
Linoleoyl-CoA + Water → Coenzyme A + Linoleic aciddetails
General function:
Involved in acyl-CoA thioesterase activity
Specific function:
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in acyltransferase activity
Specific function:
Acyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity. Required for establishment of the hematopoietic and endothelial lineages.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in thiolester hydrolase activity
Specific function:
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active towards fatty acyl-CoA with chain-lengths of C12-C16 (By similarity).
Gene Name:
Uniprot ID:
Molecular weight:
Linoleoyl-CoA + Water → Coenzyme A + Linoleic aciddetails