| Record Information |
|---|
| Version |
3.5 |
| Creation Date |
2005-11-16 08:48:42 -0700 |
| Update Date |
2013-02-08 17:10:31 -0700 |
| HMDB ID |
HMDB01423 |
| Secondary Accession Numbers |
None |
| Metabolite Identification |
|---|
| Common Name |
Coenzyme A |
| Description |
Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, notable for its role in the synthesis and oxidization of fatty acids, and the oxidation of pyruvate in the citric acid cycle. It is adapted from beta-mercaptoethylamine, panthothenate and adenosine triphosphate. Coenzyme A is synthesized in a five-step process from pantothenate and cysteine. In the first step Pantothenate (vitamin B5) is phosphorylated to 4'-phosphopantothenate by the enzyme pantothenate kinase (PanK; CoaA; CoaX)In the second step, a cysteine is added to 4'-phosphopantothenate by the enzyme phosphopantothenoylcysteine synthetase (PPC-DC; CoaB) to form 4'-phospho-N-pantothenoylcysteine (PPC). In the third step, PPC is decarboxylated to 4'-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (CoaC). In the fourth step, 4'-phosphopantetheine is adenylylated to form dephospho-CoA by the enzyme phosphopantetheine adenylyl transferase (CoaD)Finally, dephospho-CoA is phosphorylated using ATP to coenzyme A by the enzyme dephosphocoenzyme A kinase (CoaE). Since coenzyme A is, in chemical terms, a thiol, it can react with carboxylic acids to form thioesters, thus functioning as an acyl group carrier. CoA assists in transferring fatty acids from the cytoplasm to mitochondria. A molecule of coenzyme A carrying an acetyl group is also referred to as acetyl-CoA. When it is not attached to an acyl group, it is usually referred to as 'CoASH' or 'HSCoA'. Coenzyme A is also the source of the phosphopantetheine group that is added as a prosthetic group to proteins such as acyl carrier protein and formyltetrahydrofolate dehydrogenase Acetyl-CoA is an important molecule itself. It is the precursor to HMG CoA, which is a vital component in cholesterol and ketone synthesis. Furthermore, it contributes an acetyl group to choline to produce acetylcholine, in a reaction catalysed by choline acetyltransferase. Its main task is conveying the carbon atoms within the acetyl group to the citric acid cycle to be oxidized for energy production. -- Wikipedia. |
| Structure |
Download:
MOL |
SDF |
SMILES |
InChI
Display:
2D Structure |
3D Structure
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| Synonyms |
- Acetoacetyl coenzyme A sodium salt
- CoA
- CoA hydrate
- CoA-SH
- CoASH
- Coenzyme A
- Coenzyme A hydrate
- Coenzyme A-SH
- Coenzyme ASH
- Coenzymes A
- Depot-Zeel
- Propionyl CoA
- Propionyl Coenzyme A
- S-Propanoate
- S-Propanoate CoA
- S-Propanoate Coenzyme A
- S-Propanoic acid
- S-Propionate CoA
- S-Propionate Coenzyme A
- Zeel
- [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl 3-hydroxy-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate
|
| Chemical Formula |
C21H36N7O16P3S |
| Average Molecular Weight |
767.534 |
| Monoisotopic Molecular Weight |
767.115208365 |
| IUPAC Name |
{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-2-({[hydroxy({hydroxy[3-hydroxy-2,2-dimethyl-3-({2-[(2-sulfanylethyl)carbamoyl]ethyl}carbamoyl)propoxy]phosphoryl}oxy)phosphoryl]oxy}methyl)oxolan-3-yl]oxy}phosphonic acid |
| Traditional IUPAC Name |
[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-2-[({hydroxy[hydroxy(3-hydroxy-2,2-dimethyl-3-({2-[(2-sulfanylethyl)carbamoyl]ethyl}carbamoyl)propoxy)phosphoryl]oxyphosphoryl}oxy)methyl]oxolan-3-yl]oxyphosphonic acid |
| CAS Registry Number |
85-61-0 |
| 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)NCCS |
| InChI Identifier |
InChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16?,20-/m1/s1 |
| InChI Key |
RGJOEKWQDUBAIZ-DRCCLKDXSA-N |
| Chemical Taxonomy |
|---|
| Kingdom |
Organic Compounds |
| Super Class |
Nucleosides, Nucleotides, and Analogues |
| Class |
Purine Nucleotides |
| Sub Class |
Purine Ribonucleotides |
| Other Descriptors |
- Aromatic Heteropolycyclic Compounds
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| Substituents |
- 1 Phosphoribosyl Imidazole
- Alkylthiol
- Aminopyrimidine
- Carboxamide Group
- Glycosyl Compound
- Imidazole
- Imidazopyrimidine
- Monosaccharide Phosphate
- N Glycosyl Compound
- Organic Hypophosphite
- Organic Phosphite
- Organic Pyrophosphate
- Oxolane
- Pentose Monosaccharide
- Phosphoric Acid Ester
- Purine
- Purine Ribonucleoside 3',5' Bisphosphate
- Pyrimidine
- Saccharide
- Secondary Alcohol
- Secondary Carboxylic Acid Amide
- Thiol (Sulfanyl Compound)
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| Direct Parent |
Coenzyme A and Derivatives |
| Ontology |
|---|
| Status |
Expected and Not Quantified |
| Origin |
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| Biofunction |
- Component of Alanine and aspartate metabolism
- Component of Aminosugars metabolism
- Component of Arginine and proline metabolism
- Component of Bile acid biosynthesis
- Component of Butanoate metabolism
- Component of C5-Branched dibasic acid metabolism
- Component of Fatty acid metabolism
- Component of Glutamate metabolism
- Component of Glycerolipid metabolism
- Component of Glycerophospholipid metabolism
- Component of Glycine, serine and threonine metabolism
- Component of Glycosphingolipid metabolism
- Component of Glyoxylate and dicarboxylate metabolism
- Component of Inositol metabolism
- Component of Propanoate metabolism
- Component of Pyruvate metabolism
- Component of Tryptophan metabolism
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| Application |
Not Available |
| Cellular locations |
- Mitochondria
- Nucleus
- Lysosome
- Endoplasmic reticulum
- Golgi apparatus
- Peroxisome
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| Physical Properties |
|---|
| State |
Solid |
| Experimental Properties |
| Property |
Value |
Reference |
| Melting Point |
Not Available |
Not Available |
| Boiling Point |
Not Available |
Not Available |
| Water Solubility |
Not Available |
Not Available |
| LogP |
Not Available |
Not Available |
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| Predicted Properties |
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| Spectra |
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| Biological Properties |
|---|
| Cellular Locations |
- Mitochondria
- Nucleus
- Lysosome
- Endoplasmic reticulum
- Golgi apparatus
- Peroxisome
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| Biofluid Locations |
Not Available
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| Tissue Location |
- Skeletal Muscle
- Fibroblasts
- Adipose Tissue
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| Pathways |
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| Normal Concentrations |
|---|
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Not Available |
| Abnormal Concentrations |
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Not Available |
| Associated Disorders and Diseases |
|---|
| Disease References |
None |
| Associated OMIM IDs |
None |
| External Links |
|---|
| DrugBank ID |
Not Available |
| Phenol Explorer Compound ID |
Not Available |
| Phenol Explorer Metabolite ID |
Not Available |
| FoodDB ID |
FDB022614 |
| KNApSAcK ID |
Not Available |
| Chemspider ID |
6557  |
| KEGG Compound ID |
C00010 |
| BioCyc ID |
CO-A |
| BiGG ID |
33502 |
| Wikipedia Link |
Coenzyme A |
| NuGOwiki Link |
HMDB01423 |
| Metagene Link |
HMDB01423 |
| METLIN ID |
6235 |
| PubChem Compound |
6816 |
| PDB ID |
1A59 |
| ChEBI ID |
1146900 |
| References |
|---|
| Synthesis Reference |
Not Available |
| Material Safety Data Sheet (MSDS) |
Download (PDF)
|
| General References |
- Yano S, Li L, Le TP, Moseley K, Guedalia A, Lee J, Gonzalez I, Boles RG: Infantile mitochondrial DNA depletion syndrome associated with methylmalonic aciduria and 3-methylcrotonyl-CoA and propionyl-CoA carboxylase deficiencies in two unrelated patients: a new phenotype of mtDNA depletion syndrome. J Inherit Metab Dis. 2003;26(5):481-8.
Pubmed: 14518828
- Roe CR, Sweetman L, Roe DS, David F, Brunengraber H: Treatment of cardiomyopathy and rhabdomyolysis in long-chain fat oxidation disorders using an anaplerotic odd-chain triglyceride. J Clin Invest. 2002 Jul;110(2):259-69.
Pubmed: 12122118
- Kretschmer RE, Bachmann C: Methylcitric acid determination in amniotic fluid by electron-impact mass fragmentography. J Clin Chem Clin Biochem. 1988 May;26(5):345-8.
Pubmed: 3404093
- Osmundsen H, Bremer J, Pedersen JI: Metabolic aspects of peroxisomal beta-oxidation. Biochim Biophys Acta. 1991 Sep 11;1085(2):141-58.
Pubmed: 1892883
- Reihner E, Angelin B, Rudling M, Ewerth S, Bjorkhem I, Einarsson K: Regulation of hepatic cholesterol metabolism in humans: stimulatory effects of cholestyramine on HMG-CoA reductase activity and low density lipoprotein receptor expression in gallstone patients. J Lipid Res. 1990 Dec;31(12):2219-26.
Pubmed: 2090716
- Bergstrom T, Greter J, Levin AH, Steen G, Tryding N, Wass U: Propionyl-CoA carboxylase deficiency: case report, effect of low-protein diet and identification of 3-oxo-2-methylvaleric acid 3-hydroxy-2-methylvaleric acid, and maleic acid in urine. Scand J Clin Lab Invest. 1981 Apr;41(2):117-26.
Pubmed: 7313494
- Salen G, Batta AK, Tint GS, Shefer S: Comparative effects of lovastatin and chenodeoxycholic acid on plasma cholestanol levels and abnormal bile acid metabolism in cerebrotendinous xanthomatosis. Metabolism. 1994 Aug;43(8):1018-22.
Pubmed: 8052141
- Lehnert W, Junker A: [2-Methyl-3-oxovaleric acid: a characteristic metabolite in propionic acidemia] Clin Chim Acta. 1980 May 21;104(1):47-51.
Pubmed: 7389125
- Wendel U, Zass R, Leupold D: Contribution of odd-numbered fatty acid oxidation to propionate production in neonates with methylmalonic and propionic acidaemias. Eur J Pediatr. 1993 Dec;152(12):1021-3.
Pubmed: 8131803
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| Enzymes |
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| Name: |
ATP-citrate synthase
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| Reactions: |
- ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA [RN:R00352]
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| Gene Name: |
ACLY |
| Uniprot ID: |
P53396 |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Fatty acid synthase
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| Reactions: |
- a (3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = a hexadec-2-enoyl-[acyl-carrier protein] + H2O [RN:R04462]
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| Gene Name: |
FASN |
| Uniprot ID: |
P49327 |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
2-oxoglutarate dehydrogenase, mitochondrial
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| Reactions: |
- 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 [RN:R01700]
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| Gene Name: |
OGDH |
| Uniprot ID: |
Q02218 |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Bile acyl-CoA synthetase
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| Reactions: |
- (1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA [RN:R02794]
- (2) ATP + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA [RN:R04580]
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| Gene Name: |
SLC27A5 |
| Uniprot ID: |
Q9Y2P5 |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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