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Record Information
StatusExpected but not Quantified
Creation Date2006-08-12 20:30:43 UTC
Update Date2021-09-14 14:59:13 UTC
Secondary Accession Numbers
  • HMDB0006490
  • HMDB03419
  • HMDB06490
Metabolite Identification
Common NameFormyl-CoA
DescriptionFormyl-CoA, also known as formyl coenzyme A, belongs to the class of organic compounds known as coenzyme a and derivatives. These are derivative of vitamin B5 containing a 4'-phosphopantetheine moiety attached to a diphospho-adenosine. Formyl-CoA is a strong basic compound (based on its pKa). It is a temporary compound formed when coenzyme A (CoA) attaches to the end of a long-chain fatty acid inside living cells. In humans, formyl-CoA is involved in the metabolic disorder called the refsum disease pathway. Outside of the human body, formyl-CoA has been detected, but not quantified in, several different foods, such as horned melons, gingers, wild celeries, broad beans, and asparagus. This could make formyl-CoA a potential biomarker for the consumption of these foods. This, in turn, enters the citric acid cycle, eventually forming several molecules of ATP.To be oxidatively degraded, a fatty acid must first be activated in a two-step reaction catalyzed by acyl-CoA synthetase. Fatty acids are activated in the cytosol, but oxidation occurs in the mitochondria. Because there is no transport protein for CoA adducts, acyl groups must enter the mitochondria via a shuttle system involving the small molecule carnitine. Consequently, the overall reaction has a free energy change near zero:Fatty acid + CoA + ATP ⇌ Acyl-CoA + AMP + PPiSubsequent hydrolysis of the product PPi (by the enzyme inorganic pyrophosphatase) is highly exergonic, and this reaction makes the formation of acyl-CoA spontaneous and irreversible. First, the fatty acid displaces the diphosphate group of ATP, then coenzyme A (HSCoA) displaces the AMP group to form an acyl-CoA. The second step, transfer of the acyl group to CoA (the same molecule that carries acetyl groups as acetyl-CoA), conserves free energy in the formation of a thioester bond. Acyl-CoA is a group of coenzymes involved in the metabolism of fatty acids.
Formyl coenzyme AHMDB
Formyl-coenzyme AHMDB
Chemical FormulaC22H36N7O17P3S
Average Molecular Weight795.544
Monoisotopic Molecular Weight795.110122987
IUPAC Name{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-2-[({[({3-[(2-{[2-(formylsulfanyl)ethyl]carbamoyl}ethyl)carbamoyl]-3-hydroxy-2,2-dimethylpropoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)methyl]-4-hydroxyoxolan-3-yl]oxy}phosphonic acid
Traditional Name[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-2-{[({3-[(2-{[2-(formylsulfanyl)ethyl]carbamoyl}ethyl)carbamoyl]-3-hydroxy-2,2-dimethylpropoxy(hydroxy)phosphoryl}oxy(hydroxy)phosphoryl)oxy]methyl}-4-hydroxyoxolan-3-yl]oxyphosphonic acid
CAS Registry Number13131-49-2
InChI Identifier
Chemical Taxonomy
Description Belongs to the class of organic compounds known as coenzyme a and derivatives. These are derivative of vitamin B5 containing a 4'-phosphopantetheine moiety attached to a diphospho-adenosine.
KingdomOrganic compounds
Super ClassNucleosides, nucleotides, and analogues
ClassPurine nucleotides
Sub ClassPurine ribonucleotides
Direct ParentCoenzyme A and derivatives
Alternative Parents
  • Coenzyme a or derivatives
  • Purine ribonucleoside diphosphate
  • Pentose phosphate
  • Pentose-5-phosphate
  • Ribonucleoside 3'-phosphate
  • Beta amino acid or derivatives
  • Glycosyl compound
  • N-glycosyl compound
  • 6-aminopurine
  • Pentose monosaccharide
  • Organic pyrophosphate
  • Monosaccharide phosphate
  • Purine
  • Imidazopyrimidine
  • Aminopyrimidine
  • Monoalkyl phosphate
  • Monosaccharide
  • N-acyl-amine
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Pyrimidine
  • Imidolactam
  • Phosphoric acid ester
  • Fatty acyl
  • Fatty amide
  • Alkyl phosphate
  • Tetrahydrofuran
  • Heteroaromatic compound
  • Imidazole
  • Azole
  • Carbothioic s-ester
  • Thiocarboxylic acid ester
  • Secondary carboxylic acid amide
  • Secondary alcohol
  • Carboxamide group
  • Amino acid or derivatives
  • Thiocarboxylic acid or derivatives
  • Organoheterocyclic compound
  • Azacycle
  • Oxacycle
  • Sulfenyl compound
  • Carboxylic acid derivative
  • Hydrocarbon derivative
  • Alcohol
  • Organic nitrogen compound
  • Amine
  • Organonitrogen compound
  • Carbonyl group
  • Organooxygen compound
  • Organosulfur compound
  • Organic oxygen compound
  • Organopnictogen compound
  • Primary amine
  • Organic oxide
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External DescriptorsNot Available

Route of exposure:



Naturally occurring process:

Physical Properties
Experimental Properties
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogP-3.783Not Available
Predicted Properties
Water Solubility4.47 g/LALOGPS
pKa (Strongest Acidic)0.83ChemAxon
pKa (Strongest Basic)4.95ChemAxon
Physiological Charge-4ChemAxon
Hydrogen Acceptor Count17ChemAxon
Hydrogen Donor Count9ChemAxon
Polar Surface Area363.63 ŲChemAxon
Rotatable Bond Count20ChemAxon
Refractivity167.72 m³·mol⁻¹ChemAxon
Polarizability68.93 ųChemAxon
Number of Rings3ChemAxon
Rule of FiveNoChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleYesChemAxon


Spectrum TypeDescriptionSplash KeyDeposition DateView
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0002-9243455200-7fe33bf6d4a771fe58062017-11-06View Spectrum
MSMass Spectrum (Electron Ionization)splash10-0002-9243455200-7fe33bf6d4a771fe58062021-09-05View Spectrum


Spectrum TypeDescriptionSplash KeyDeposition DateView
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-1910000300-55d9e03540fe476863952017-09-01View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-1930000000-f7d8ae48e314d038f7b22017-09-01View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-2910000000-b160c588de2d041e4b802017-09-01View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-003r-5820231900-1838b37d7ea4f52f4b462017-09-01View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-003r-3910100100-933e5170643e8bcc224c2017-09-01View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-057i-5900000000-7b6b8f24e737e82fc12e2017-09-01View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0006-0000000900-9964bca7fa7ce013e5112021-09-06View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0032-2100003900-ec87a8b97c33e09176bb2021-09-06View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-002b-9002417200-07e062501318a903fb232021-09-06View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0002-0300000900-581000df4cf64f4f53932021-09-07View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-1910000200-eab4676c05a4b9c71eae2021-09-07View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-1490000000-0296bea622f0a9d9f65c2021-09-07View Spectrum
Biological Properties
Cellular LocationsNot Available
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 IDFDB023169
KNApSAcK IDNot Available
Chemspider ID388444
KEGG Compound IDC00798
BioCyc IDNot Available
BiGG ID36030
Wikipedia LinkAcyl-CoA
METLIN IDNot Available
PubChem Compound439313
PDB IDNot Available
ChEBI ID15522
Food Biomarker OntologyNot Available
VMH IDNot Available
MarkerDB IDNot Available
Synthesis Referenceonsson, Stefan; Ricagno, Stefano; Lindqvist, Ylva; Richards, Nigel G. J. Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes. Journal of Biological Chemistry (2004), 279(34), 36003-36012.
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Croes K, Casteels M, Asselberghs S, Herdewijn P, Mannaerts GP, Van Veldhoven PP: Formation of a 2-methyl-branched fatty aldehyde during peroxisomal alpha-oxidation. FEBS Lett. 1997 Aug 4;412(3):643-5. [PubMed:9276483 ]
  2. Croes K, Van Veldhoven PP, Mannaerts GP, Casteels M: Production of formyl-CoA during peroxisomal alpha-oxidation of 3-methyl-branched fatty acids. FEBS Lett. 1997 Apr 28;407(2):197-200. [PubMed:9166898 ]

Only showing the first 10 proteins. There are 15 proteins in total.


General function:
Involved in 5-aminolevulinate synthase activity
Specific function:
Not Available
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in 5-aminolevulinate synthase activity
Specific function:
Not Available
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in uroporphyrinogen decarboxylase activity
Specific function:
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in coproporphyrinogen oxidase activity
Specific function:
Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in uroporphyrinogen-III synthase activity
Specific function:
Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme).
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in hydroxymethylbilane synthase activity
Specific function:
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in biliverdin reductase activity
Specific function:
Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in catalytic activity
Specific function:
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in ferrochelatase activity
Specific function:
Catalyzes the ferrous insertion into protoporphyrin IX.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in porphobilinogen synthase activity
Specific function:
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
Gene Name:
Uniprot ID:
Molecular weight:

Only showing the first 10 proteins. There are 15 proteins in total.