malonyl-CoA (PAMDB110387)

IdentificationTaxonomyPhysical PropertiesBiological PropertiesSpectraConcentrationsLinksReferencesEnzymes Transporters
Proteins (3280)
Record Information
Version 1.0
Update Date 1/22/2018 11:54:54 AM
Metabolite IDPAMDB110387
Identification
Name: malonyl-CoA
Description:Pentaanion of malonyl-CoA arising from deprotonation of phosphate, diphosphate and carboxylic acid functions.
Structure
Thumb
🔍MOLSDFPDBSMILESInChIView Structure
Synonyms:
  • malonyl coenzyme A
Chemical Formula: C24H33N7O19P3S
Average Molecular Weight: 848.54
Monoisotopic Molecular Weight: 853.1156022961
InChI Key: LTYOQGRJFJAKNA-DVVLENMVSA-I
InChI: InChI=1S/C24H38N7O19P3S/c1-24(2,19(37)22(38)27-4-3-13(32)26-5-6-54-15(35)7-14(33)34)9-47-53(44,45)50-52(42,43)46-8-12-18(49-51(39,40)41)17(36)23(48-12)31-11-30-16-20(25)28-10-29-21(16)31/h10-12,17-19,23,36-37H,3-9H2,1-2H3,(H,26,32)(H,27,38)(H,33,34)(H,42,43)(H,44,45)(H2,25,28,29)(H2,39,40,41)/p-5/t12-,17-,18-,19+,23-/m1/s1
CAS number: 524-14-1
IUPAC Name:3'-phosphonatoadenosine 5'-{3-[(3R)-4-{[3-({2-[(3-carboxylatoacetyl)sulfanyl]ethyl}amino)-3-oxopropyl]amino}-3-hydroxy-2,2-dimethyl-4-oxobutyl] diphosphate}
Traditional IUPAC Name: 3-({2-[3-(3-{[({[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy(hydroxy)phosphoryl}oxy(hydroxy)phosphoryl)oxy]methyl}-2-hydroxy-3-methylbutanamido)propanamido]ethyl}sulfanyl)-3-oxopropanoic acid
SMILES:CC(C)(C(O)C(=O)NCCC(=O)NCCSC(=O)CC(=O)[O-])COP(=O)(OP(=O)(OCC1(C(OP([O-])(=O)[O-])C(O)C(O1)N3(C2(=C(C(N)=NC=N2)N=C3))))[O-])[O-]
Chemical Taxonomy
Taxonomy DescriptionThis compound belongs to the class of chemical entities known as acyl coas. These are organic compounds containing a coenzyme A substructure linked to an acyl chain.
Kingdom Chemical entities
Super ClassOrganic compounds
Class Lipids and lipid-like molecules
Sub ClassFatty Acyls
Direct Parent Acyl CoAs
Alternative Parents
Substituents
  • Coenzyme a or derivatives
  • Purine ribonucleoside 3',5'-bisphosphate
  • Purine ribonucleoside bisphosphate
  • Purine ribonucleoside diphosphate
  • Pentose phosphate
  • Pentose-5-phosphate
  • Ribonucleoside 3'-phosphate
  • Beta amino acid or derivatives
  • Glycosyl compound
  • N-glycosyl compound
  • Monosaccharide phosphate
  • Organic pyrophosphate
  • 6-aminopurine
  • Pentose monosaccharide
  • Imidazopyrimidine
  • Purine
  • Monoalkyl phosphate
  • Aminopyrimidine
  • Fatty amide
  • Imidolactam
  • Monosaccharide
  • N-acyl-amine
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Alkyl phosphate
  • 1,3-dicarbonyl compound
  • Phosphoric acid ester
  • Primary aromatic amine
  • Pyrimidine
  • Oxolane
  • Azole
  • Imidazole
  • Heteroaromatic compound
  • Secondary carboxylic acid amide
  • Amino acid or derivatives
  • Secondary alcohol
  • Thiocarboxylic acid ester
  • Carboxamide group
  • Carbothioic s-ester
  • Amino acid
  • Oxacycle
  • Organoheterocyclic compound
  • Azacycle
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Carboxylic acid derivative
  • Sulfenyl compound
  • Thiocarboxylic acid or derivatives
  • Hydrocarbon derivative
  • Organic nitrogen compound
  • Alcohol
  • Amine
  • Organonitrogen compound
  • Carbonyl group
  • Organooxygen compound
  • Organosulfur compound
  • Organic oxygen compound
  • Organopnictogen compound
  • Primary amine
  • Organic oxide
  • Aromatic heteropolycyclic compound
Molecular Framework Aromatic heteropolycyclic compounds
External Descriptors Not Available
Physical Properties
State: Solid
Charge:-5
Melting point: Not Available
Experimental Properties:
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Water Solubility3.8 mg/mLALOGPS
logP-0.62ALOGPS
logP-7.1ChemAxon
logS-2.4ALOGPS
pKa (Strongest Acidic)0.82ChemAxon
pKa (Strongest Basic)4.97ChemAxon
Physiological Charge-5ChemAxon
Hydrogen Acceptor Count19ChemAxon
Hydrogen Donor Count10ChemAxon
Polar Surface Area400.93 Å2ChemAxon
Rotatable Bond Count22ChemAxon
Refractivity178.55 m3·mol-1ChemAxon
Polarizability74.29 Å3ChemAxon
Number of Rings3ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations: Not Available
Reactions:
malonyl-CoA → coenzyme A
ATP + acetyl-CoA + Water → malonyl-CoA + ADP + phosphate + Hydrogen ion
malonyl-CoA + Hydrogen ion → Carbon dioxide + coenzyme A
ATP + acetyl-CoA + Hydrogen carbonate → Hydrogen ion + malonyl-CoA + phosphate + ADP
Pathways:
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, NegativeNot Available
References
References:
  • Roepstorff C, Halberg N, Hillig T, Saha AK, Ruderman NB, Wojtaszewski JF, Richter EA, Kiens B: Malonyl-CoA and carnitine in regulation of fat oxidation in human skeletal muscle during exercise. Am J Physiol Endocrinol Metab. 2005 Jan;288(1):E133-42. Epub 2004 Sep 21. [15383373 ]
  • Napal L, Dai J, Treber M, Haro D, Marrero PF, Woldegiorgis G: A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzyme. J Biol Chem. 2003 Sep 5;278(36):34084-9. Epub 2003 Jun 25. [12826662 ]
  • Kuhl JE, Ruderman NB, Musi N, Goodyear LJ, Patti ME, Crunkhorn S, Dronamraju D, Thorell A, Nygren J, Ljungkvist O, Degerblad M, Stahle A, Brismar TB, Andersen KL, Saha AK, Efendic S, Bavenholm PN: Exercise training decreases the concentration of malonyl-CoA and increases the expression and activity of malonyl-CoA decarboxylase in human muscle. Am J Physiol Endocrinol Metab. 2006 Jun;290(6):E1296-303. Epub 2006 Jan 24. [16434556 ]
  • Odland LM, Howlett RA, Heigenhauser GJ, Hultman E, Spriet LL: Skeletal muscle malonyl-CoA content at the onset of exercise at varying power outputs in humans. Am J Physiol. 1998 Jun;274(6 Pt 1):E1080-5. [9611159 ]
  • Bandyopadhyay GK, Yu JG, Ofrecio J, Olefsky JM: Increased malonyl-CoA levels in muscle from obese and type 2 diabetic subjects lead to decreased fatty acid oxidation and increased lipogenesis; thiazolidinedione treatment reverses these defects. Diabetes. 2006 Aug;55(8):2277-85. [16873691 ]
  • Pender C, Trentadue AR, Pories WJ, Dohm GL, Houmard JA, Youngren JF: Expression of genes regulating malonyl-CoA in human skeletal muscle. J Cell Biochem. 2006 Oct 15;99(3):860-7. [16721829 ]
  • Prentki M, Corkey BE: Are the beta-cell signaling molecules malonyl-CoA and cystolic long-chain acyl-CoA implicated in multiple tissue defects of obesity and NIDDM? Diabetes. 1996 Mar;45(3):273-83. [8593930 ]
  • Bavenholm PN, Pigon J, Saha AK, Ruderman NB, Efendic S: Fatty acid oxidation and the regulation of malonyl-CoA in human muscle. Diabetes. 2000 Jul;49(7):1078-83. [10909961 ]
  • Ruderman NB, Saha AK, Vavvas D, Witters LA: Malonyl-CoA, fuel sensing, and insulin resistance. Am J Physiol. 1999 Jan;276(1 Pt 1):E1-E18. [9886945 ]
  • Saha AK, Ruderman NB: Malonyl-CoA and AMP-activated protein kinase: an expanding partnership. Mol Cell Biochem. 2003 Nov;253(1-2):65-70. [14619957 ]
  • Morillas M, Gomez-Puertas P, Bentebibel A, Selles E, Casals N, Valencia A, Hegardt FG, Asins G, Serra D: Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for malonyl-CoA inhibition. Mutation of methionine 593 abolishes malonyl-CoA inhibition. J Biol Chem. 2003 Mar 14;278(11):9058-63. Epub 2002 Dec 23. [12499375 ]
  • Odland LM, Heigenhauser GJ, Lopaschuk GD, Spriet LL: Human skeletal muscle malonyl-CoA at rest and during prolonged submaximal exercise. Am J Physiol. 1996 Mar;270(3 Pt 1):E541-4. [8638703 ]
  • Trevisan CP, Angelini C, Fiorellini LA, Isaya G, Zacchello G: Malonyl-CoA abnormal inhibition of residual enzyme activity in carnitine palmitoyltransferase deficiency. Eur Neurol. 1986;25(4):309-16. [3720808 ]
Synthesis Reference: Hulsmann, W. C. Synthesis of malonyl coenzyme A from acetyl coenzyme A and oxalosuccinate in mitochondria. Biochimica et Biophysica Acta (1963), 77(3), 502-3.
Material Safety Data Sheet (MSDS) Not Available
External Links:
ResourceLink
CAS524-14-1
ChEBI57384
HMDBHMDB01175
IAF126033789
KEGGC00083
MetaboLightsMTBLC57384
PubChem25246281