Structural search and advanced query search is temporarily unavailable. We are working to fix this issue. Thank you for your support and patience.


Hexanoyl-CoA (M2MDB000467)

Record Information
Version2.0
Creation Date2012-05-31 13:57:11 -0600
Update Date2015-10-15 16:14:00 -0600
Secondary Accession Numbers
  • ECMDB02845
Identification
Name:Hexanoyl-CoA
DescriptionHexanoyl-CoA is a fatty acid coenzyme A derivative that can be involved in the biosynthesis and oxidation of fatty acids.
Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms:
  • 6-Carboxyhexanoyl-CoA
  • 6-Carboxyhexanoyl-Coenzyme A
  • Caproyl-CoA
  • Caproyl-Coenzyme A
  • Hexanoyl-coenzyme A
  • Pimeloyl-CoA
  • Pimeloyl-Coenzyme A
Chemical Formula:C27H46N7O17P3S
Weight:Average: 865.677
Monoisotopic: 865.188373307
InChI Key:OEXFMSFODMQEPE-UHFFFAOYSA-N
InChI:InChI=1S/C27H46N7O17P3S/c1-4-5-6-7-18(36)55-11-10-29-17(35)8-9-30-25(39)22(38)27(2,3)13-48-54(45,46)51-53(43,44)47-12-16-21(50-52(40,41)42)20(37)26(49-16)34-15-33-19-23(28)31-14-32-24(19)34/h14-16,20-22,26,37-38H,4-13H2,1-3H3,(H,29,35)(H,30,39)(H,43,44)(H,45,46)(H2,28,31,32)(H2,40,41,42)
CAS number:5060-32-2
IUPAC Name:{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-2-({[({[(3R)-3-[(2-{[2-(hexanoylsulfanyl)ethyl]carbamoyl}ethyl)carbamoyl]-3-hydroxy-2,2-dimethylpropoxy](hydroxy)phosphoryl}oxy)(hydroxy)phosphoryl]oxy}methyl)-4-hydroxyoxolan-3-yl]oxy}phosphonic acid
Traditional IUPAC Name:hexanoyl-coa
SMILES:CCCCCC(=O)SCCN=C(O)CCN=C(O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12
Chemical Taxonomy
Description belongs to the class of organic compounds known as 2,3,4-saturated fatty acyl coas. These are acyl-CoAs carrying a 2,3,4-saturated fatty acyl chain.
KingdomOrganic compounds
Super ClassLipids and lipid-like molecules
ClassFatty Acyls
Sub ClassFatty acyl thioesters
Direct Parent2,3,4-saturated fatty acyl CoAs
Alternative Parents
Substituents
  • 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
Physical Properties
State:Solid
Charge:-4
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility3.67 g/LALOGPS
logP0.07ALOGPS
logP-3.8ChemAxon
logS-2.4ALOGPS
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 Count24ChemAxon
Refractivity190.64 m³·mol⁻¹ChemAxon
Polarizability80.88 ųChemAxon
Number of Rings3ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
Adenosine triphosphate + Coenzyme A + Hydrogen ion + Hexanoate (N-C6:0) > Adenosine monophosphate + Hydrogen ion + Hexanoyl-CoA + Pyrophosphate
Acetyl-CoA + Hexanoate (N-C6:0) > Acetic acid + Hexanoyl-CoA
Acetyl-CoA + Hexanoyl-CoA <> 3-Oxooctanoyl-CoA + Coenzyme A
FAD + Hexanoyl-CoA <> FADH2 + trans-2-Hexenoyl-CoA
Water + Hexanoyl-CoA > Coenzyme A + Hydrogen ion + Hexanoate (N-C6:0)
SMPDB Pathways:
Fatty acid metabolismPW000796 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways:
EcoCyc Pathways:Not Available
Concentrations
Not Available
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000j-1931000110-940fe882d4b8cefb1914View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0079-1921000000-de60fcd8bc6f0c9bf08dView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0079-1910000000-29936f42a08315dcc8ffView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-01rt-7911042450-6db5d278813c82f99785View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001i-4901110010-64b9e09e0fd795b938c8View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-056r-8900100000-f1097e6a0dd8990fbfb7View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-03di-0000000090-5cc3f6bd431e230faf4aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-03gj-9600204660-0d998b9d3d0254c489f4View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-00p0-7104802930-08e206f3a7fa95fa94d3View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-014i-0000000190-fde2b5c220974cde750cView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-1901001680-96f2a80cee26fb36881bView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a4i-0119000000-74dda344be4f5c2e3b01View in MoNA
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
References
References:
  • Dugan RE, Schmidt MJ, Hoganson GE, Steele J, Gilles BA, Shug AL: High-performance liquid chromatography of coenzyme A esters formed by transesterification of short-chain acylcarnitines: diagnosis of acidemias by urinary analysis. Anal Biochem. 1987 Feb 1;160(2):275-80. Pubmed: 3578754
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064
Synthesis Reference:Pullman, Maynard E. Convenient and versatile method for the purification of CoA thiol esters. Analytical Biochemistry (1973), 54(1), 188-98.
Material Safety Data Sheet (MSDS)Not Available
External Links:
ResourceLink
CHEBI ID27540
HMDB IDHMDB02845
Pubchem Compound ID440611
Kegg IDC05270
ChemSpider ID389509
Wikipedia IDNot Available
BioCyc IDHEXANOYL-COA
EcoCyc IDHEXANOYL-COA

Enzymes

Protein Details
1. 3-ketoacyl-CoA thiolase
General function:
Involved in acetyl-CoA C-acyltransferase activity
Specific function:
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids
Gene Name:
fadA
Uniprot ID:
P21151
Molecular weight:
40876
Reactions
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
Protein Details
2. Long-chain-fatty-acid--CoA ligase
General function:
Involved in catalytic activity
Specific function:
Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids
Gene Name:
fadD
Uniprot ID:
P69451
Molecular weight:
62332
Reactions
ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.
Protein Details
3. Acetate CoA-transferase subunit alpha
General function:
Involved in CoA-transferase activity
Specific function:
Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA
Gene Name:
atoD
Uniprot ID:
P76458
Molecular weight:
23526
Reactions
Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA.
Protein Details
4. Acetate CoA-transferase subunit beta
General function:
Involved in CoA-transferase activity
Specific function:
Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA
Gene Name:
atoA
Uniprot ID:
P76459
Molecular weight:
22960
Reactions
Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA.
Protein Details
5. 3-ketoacyl-CoA thiolase_
General function:
Involved in transferase activity
Specific function:
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long- chain fatty acids
Gene Name:
fadI
Uniprot ID:
P76503
Molecular weight:
46530
Reactions
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
Protein Details
6. Acyl-coenzyme A dehydrogenase
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Catalyzes the dehydrogenation of acyl-CoA
Gene Name:
fadE
Uniprot ID:
Q47146
Molecular weight:
89224
Reactions
An acyl-CoA + FAD = a dehydrogenated acyl-CoA + FADH(2).
Protein Details
7. Short-chain-fatty-acid--CoA ligase
General function:
Involved in catalytic activity
Specific function:
Catalyzes the esterification, concomitant with transport, of exogenous fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. It has a low activity on medium or long chain fatty acids and is maximally active on C6 and C8 substrates
Gene Name:
fadK
Uniprot ID:
P38135
Molecular weight:
60773
Reactions
ATP + a short-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
Protein Details
8. Acyl-CoA thioesterase 2
General function:
Involved in acyl-CoA hydrolase activity
Specific function:
Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known
Gene Name:
tesB
Uniprot ID:
P0AGG2
Molecular weight:
31966