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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2016-02-11 01:03:57 UTC
HMDB IDHMDB01175
Secondary Accession NumbersNone
Metabolite Identification
Common NameMalonyl-CoA
DescriptionMalonyl-CoA is a coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.
Structure
Thumb
Synonyms
ValueSource
Malonyl CoAHMDB
Malonyl coenzyme AHMDB
Malonyl-coenzyme AHMDB
Omega-carboxyacyl-CoAHMDB
Omega-carboxyacyl-coenzyme AHMDB
S-(Hydrogen malonyl)coenzyme AHMDB
S-(Hydrogen propanedioateHMDB
S-(Hydrogen propanedioate) CoAHMDB
S-(Hydrogen propanedioate) coenzyme AHMDB
S-(Hydrogen propanedioic acidHMDB
Chemical FormulaC24H38N7O19P3S
Average Molecular Weight853.58
Monoisotopic Molecular Weight853.115602295
IUPAC Name3-{[2-(3-{3-[({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-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
Traditional Name3-({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
CAS Registry Number524-14-1
SMILES
CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)C(O)C(=O)NCCC(=O)NCCSC(=O)CC(O)=O
InChI Identifier
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)/t12-,17-,18-,19?,23-/m1/s1
InChI KeyInChIKey=LTYOQGRJFJAKNA-VFLPNFFSSA-N
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as acyl coas. These are organic compounds containing a coenzyme A substructure linked to an acyl chain.
KingdomOrganic compounds
Super ClassLipids and lipid-like molecules
ClassFatty Acyls
Sub ClassFatty acyl thioesters
Direct ParentAcyl CoAs
Alternative Parents
Substituents
  • Coenzyme a or derivatives
  • Purine ribonucleoside diphosphate
  • Purine ribonucleoside 3',5'-bisphosphate
  • N-glycosyl compound
  • Glycosyl compound
  • Beta amino acid or derivatives
  • Organic pyrophosphate
  • Monosaccharide phosphate
  • 6-aminopurine
  • Purine
  • Imidazopyrimidine
  • Monoalkyl phosphate
  • Aminopyrimidine
  • Imidolactam
  • Alkyl phosphate
  • 1,3-dicarbonyl compound
  • Pyrimidine
  • Primary aromatic amine
  • Phosphoric acid ester
  • Organic phosphoric acid derivative
  • Organic phosphate
  • N-substituted imidazole
  • N-acyl-amine
  • Monosaccharide
  • Fatty amide
  • Saccharide
  • Heteroaromatic compound
  • Oxolane
  • Imidazole
  • Azole
  • Thiocarboxylic acid ester
  • Secondary carboxylic acid amide
  • Secondary alcohol
  • Carboxamide group
  • Oxacycle
  • Azacycle
  • Organoheterocyclic compound
  • Sulfenyl compound
  • Thioether
  • Thiocarboxylic acid or derivatives
  • Monocarboxylic acid or derivatives
  • Carboxylic acid
  • Carboxylic acid derivative
  • Carboxylic acid amide
  • Hydrocarbon derivative
  • Primary amine
  • Organosulfur compound
  • Organooxygen compound
  • Organonitrogen compound
  • Carbonyl group
  • Amine
  • Alcohol
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External DescriptorsNot Available
Ontology
StatusExpected but not Quantified
Origin
  • Endogenous
  • Food
Biofunction
  • Cell signaling
  • Component of Propanoate metabolism
  • Component of Pyruvate metabolism
  • Component of Tetracycline biosynthesis
  • Component of beta-Alanine metabolism
  • Fuel and energy storage
  • Fuel or energy source
  • Membrane integrity/stability
Application
  • Nutrients
  • Stabilizers
  • Surfactants and Emulsifiers
Cellular locations
  • Extracellular
  • Membrane
  • Mitochondria
  • Peroxisome
Physical Properties
StateSolid
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
Spectra
SpectraNot Available
Biological Properties
Cellular Locations
  • Extracellular
  • Membrane
  • Mitochondria
  • Peroxisome
Biofluid LocationsNot Available
Tissue Location
  • Adipose Tissue
  • Fibroblasts
  • Liver
  • Muscle
  • Pancreas
  • Skeletal Muscle
Pathways
NameSMPDB LinkKEGG Link
Fatty Acid BiosynthesisSMP00456Not Available
Leigh SyndromeSMP00196Not Available
Malonic AciduriaSMP00198Not Available
Malonyl-coa decarboxylase deficiencySMP00502Not Available
Methylmalonic Aciduria Due to Cobalamin-Related DisordersSMP00201Not Available
Primary hyperoxaluria II, PH2SMP00558Not Available
Propanoate MetabolismSMP00016map00640
Pyruvate Decarboxylase E1 Component Deficiency (PDHE1 Deficiency)SMP00334Not Available
Pyruvate Dehydrogenase Complex DeficiencySMP00212Not Available
Pyruvate kinase deficiencySMP00559Not Available
Pyruvate MetabolismSMP00060map00620
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDDB04524
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB001606
KNApSAcK IDC00007260
Chemspider ID10213
KEGG Compound IDC00083
BioCyc IDMALONYL-COA
BiGG ID33789
Wikipedia LinkMalonyl-CoA
NuGOwiki LinkHMDB01175
Metagene LinkHMDB01175
METLIN ID6056
PubChem Compound10663
PDB IDNot Available
ChEBI ID15531
References
Synthesis ReferenceHulsmann, 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
General References
  1. 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 ]
  2. 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 ]
  3. 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 ]
  4. 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 ]
  5. 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 ]
  6. 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 ]
  7. 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 ]
  8. 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 ]
  9. 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 ]
  10. 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 ]
  11. 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 ]
  12. 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 ]
  13. 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 ]

Enzymes

General function:
Involved in malonyl-CoA decarboxylase activity
Specific function:
Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids.
Gene Name:
MLYCD
Uniprot ID:
O95822
Molecular weight:
55002.94
Reactions
Malonyl-CoA → Acetyl-CoA + CO(2)details
Malonyl-CoA → Acetyl-CoA + Carbon dioxidedetails
General function:
Involved in acetyl-CoA carboxylase activity
Specific function:
ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Gene Name:
ACACB
Uniprot ID:
O00763
Molecular weight:
276538.575
Reactions
Adenosine triphosphate + Acetyl-CoA + Carbonic acid → ADP + Phosphoric acid + Malonyl-CoAdetails
Acetyl-CoA + Carboxybiotin-carboxyl-carrier protein → Malonyl-CoA + Holo-[carboxylase]details
General function:
Involved in transferase activity
Specific function:
Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.
Gene Name:
FASN
Uniprot ID:
P49327
Molecular weight:
273424.06
Reactions
Malonyl-CoA + [acyl-carrier-protein] → Coenzyme A + malonyl-[acyl-carrier-protein]details
Malonyl-CoA + Acyl-carrier protein → Coenzyme A + Malonyl-[acyl-carrier protein]details
General function:
Involved in acetyl-CoA carboxylase activity
Specific function:
Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Gene Name:
ACACA
Uniprot ID:
Q13085
Molecular weight:
269997.01
Reactions
Adenosine triphosphate + Acetyl-CoA + Carbonic acid → ADP + Phosphoric acid + Malonyl-CoAdetails
Acetyl-CoA + Carboxybiotin-carboxyl-carrier protein → Malonyl-CoA + Holo-[carboxylase]details
General function:
Involved in oxidoreductase activity
Specific function:
Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.
Gene Name:
ALDH6A1
Uniprot ID:
Q02252
Molecular weight:
57839.31
Reactions
Malonic semialdehyde + Coenzyme A + NADP → Malonyl-CoA + NADPH + Hydrogen Iondetails
General function:
Involved in transferase activity
Specific function:
Catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondrias.
Gene Name:
MCAT
Uniprot ID:
Q8IVS2
Molecular weight:
19175.775
Reactions
Malonyl-CoA + [acyl-carrier-protein] → Coenzyme A + malonyl-[acyl-carrier-protein]details
Malonyl-CoA + Acyl-carrier protein → Coenzyme A + Malonyl-[acyl-carrier protein]details
General function:
Involved in G-protein coupled photoreceptor activity
Specific function:
Condensing enzyme that elongates saturated and monounsaturated very long chain fatty acids (VLCFAs). Elongates C24:0 and C26:0 acyl-CoAs. Seems to represent a photoreceptor-specific component of the fatty acid elongation system residing on the endoplasmic reticulum. May be implicated in docosahexaenoic acid (DHA) biosynthesis, which requires dietary consumption of the essential alpha-linolenic acid and a subsequent series of three elongation steps. May play a critical role in early brain and skin development.
Gene Name:
ELOVL4
Uniprot ID:
Q9GZR5
Molecular weight:
36828.905
Reactions
A very-long-chain acyl-CoA + Malonyl-CoA → Coenzyme A + a very-long-chain 3-oxoacyl-CoA + CO(2)details
Malonyl-CoA + Acyl-CoA → 3-Oxoacyl-CoA + Coenzyme A + Carbon dioxidedetails
General function:
Involved in transferase activity
Specific function:
Not Available
Gene Name:
MCAT
Uniprot ID:
B0QY72
Molecular weight:
19175.8
General function:
Involved in fatty acid biosynthetic process
Specific function:
Condensing enzyme that catalyzes the synthesis of polyunsaturated very long chain fatty acid (C20- and C22-PUFA). Acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n-6) acyl-CoA.
Gene Name:
ELOVL2
Uniprot ID:
Q9NXB9
Molecular weight:
34584.435
Reactions
A very-long-chain acyl-CoA + Malonyl-CoA → Coenzyme A + a very-long-chain 3-oxoacyl-CoA + CO(2)details
Malonyl-CoA + Acyl-CoA → 3-Oxoacyl-CoA + Coenzyme A + Carbon dioxidedetails
General function:
Involved in protein binding
Specific function:
Condensing enzyme that catalyzes the synthesis of both saturated and monounsaturated very long chain fatty acids. Exhibits activity toward saturated C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis.
Gene Name:
ELOVL1
Uniprot ID:
Q9BW60
Molecular weight:
32662.49
Reactions
A very-long-chain acyl-CoA + Malonyl-CoA → Coenzyme A + a very-long-chain 3-oxoacyl-CoA + CO(2)details
Malonyl-CoA + Acyl-CoA → 3-Oxoacyl-CoA + Coenzyme A + Carbon dioxidedetails
General function:
Not Available
Specific function:
Condensing enzyme that elongates saturated and monounsaturated very long chain fatty acids (VLCFAs). Highest activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs.
Gene Name:
ELOVL3
Uniprot ID:
Q9HB03
Molecular weight:
31500.285
Reactions
A very-long-chain acyl-CoA + Malonyl-CoA → Coenzyme A + a very-long-chain 3-oxoacyl-CoA + CO(2)details
Malonyl-CoA + Acyl-CoA → 3-Oxoacyl-CoA + Coenzyme A + Carbon dioxidedetails
General function:
Not Available
Specific function:
Condensing enzyme that catalyzes the synthesis of monounsaturated and of polyunsaturated very long chain fatty acids Acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA.
Gene Name:
ELOVL5
Uniprot ID:
Q9NYP7
Molecular weight:
38402.505
Reactions
A very-long-chain acyl-CoA + Malonyl-CoA → Coenzyme A + a very-long-chain 3-oxoacyl-CoA + CO(2)details
Malonyl-CoA + Acyl-CoA → 3-Oxoacyl-CoA + Coenzyme A + Carbon dioxidedetails
General function:
Not Available
Specific function:
Condensing enzyme that catalyzes the synthesis of saturated and monounsaturated fatty acids. Highest activity toward C16:0 acyl-CoAs.
Gene Name:
ELOVL6
Uniprot ID:
Q9H5J4
Molecular weight:
31375.81
Reactions
A very-long-chain acyl-CoA + Malonyl-CoA → Coenzyme A + a very-long-chain 3-oxoacyl-CoA + CO(2)details
Malonyl-CoA + hexadecanoyl-CoA → 3-Oxooctadecanoyl-CoA + Coenzyme A + Carbon dioxidedetails
Malonyl-CoA + Acyl-CoA → 3-Oxoacyl-CoA + Coenzyme A + Carbon dioxidedetails
General function:
Not Available
Specific function:
Condensing enzyme that catalyzes the synthesis of saturated and polyunsaturated very long chain fatty acids. Highest activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs.
Gene Name:
ELOVL7
Uniprot ID:
A1L3X0
Molecular weight:
33356.06
Reactions
A very-long-chain acyl-CoA + Malonyl-CoA → Coenzyme A + a very-long-chain 3-oxoacyl-CoA + CO(2)details
Malonyl-CoA + Acyl-CoA → 3-Oxoacyl-CoA + Coenzyme A + Carbon dioxidedetails