ECMDB: Palmityl-CoA (ECMDB01338) (M2MDB000343)

Identification Taxonomy Physical Properties Biological Properties Spectra Concentrations Links References Enzymes (6)XML

Proteins (1205)

Record Information

Version

2.0

Creation Date

2012-05-31 13:50:11 -0600

Update Date

2015-09-13 12:56:10 -0600

Secondary Accession Numbers

ECMDB01338

Identification

Name:

Palmityl-CoA

Description

Palmityl-CoA is fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.

Structure

MOL SDF PDB SMILES InChI

Synonyms:

Hexadecanoyl CoA
Hexadecanoyl Coenzyme A
Palmitoyl CoA
Palmitoyl coenzyme a
Palmitoyl-CoA
Palmitoyl-CoA (N-C16:0CoA)
Palmitoyl-Coenzyme A
Palmityl-CoA
Palmityl-Coenzyme A
S-Hexadecanoate
S-Hexadecanoate CoA
S-Hexadecanoate Coenzyme A
S-Hexadecanoic acid
S-Hexadecanoic acid CoA
S-Hexadecanoic acid Coenzyme A
S-Palmitoylcoenzyme a

Chemical Formula:

C₃₇H₆₆N₇O₁₇P₃S

Weight:

Average: 1005.943
Monoisotopic: 1005.344873947

InChI Key:

MNBKLUUYKPBKDU-TZIIWEFPSA-N

InChI:

InChI=1S/C37H66N7O17P3S/c1-4-5-6-7-8-9-10-11-12-13-14-15-16-17-28(46)65-21-20-39-27(45)18-19-40-35(49)32(48)37(2,3)23-58-64(55,56)61-63(53,54)57-22-26-31(60-62(50,51)52)30(47)36(59-26)44-25-43-29-33(38)41-24-42-34(29)44/h24-26,30-32,36,47-48H,4-23H2,1-3H3,(H,39,45)(H,40,49)(H,53,54)(H,55,56)(H2,38,41,42)(H2,50,51,52)/t26-,30-,31-,32?,36-/m1/s1

CAS number:

1763-10-6

IUPAC Name:

{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-2-[({[({3-[(2-{[2-(hexadecanoylsulfanyl)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:

[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-2-{[({3-[(2-{[2-(hexadecanoylsulfanyl)ethyl]carbamoyl}ethyl)carbamoyl]-3-hydroxy-2,2-dimethylpropoxy(hydroxy)phosphoryl}oxy(hydroxy)phosphoryl)oxy]methyl}-4-hydroxyoxolan-3-yl]oxyphosphonic acid

SMILES:

CCCCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(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

Chemical Taxonomy

Description

belongs to the class of organic compounds known as long-chain fatty acyl coas. These are acyl CoAs where the group acylated to the coenzyme A moiety is a long aliphatic chain of 13 to 21 carbon atoms.

Kingdom

Organic compounds

Super Class

Lipids and lipid-like molecules

Class

Fatty Acyls

Sub Class

Fatty acyl thioesters

Direct Parent

Long-chain 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 Framework

Aromatic heteropolycyclic compounds

External Descriptors

Fatty acyl CoAs (C00154 )

Physical Properties

State:

Solid

Charge:

-4

Melting point:

Not Available

Experimental Properties:

Property	Value	Source

Predicted Properties

Property	Value	Source
Water Solubility	1.74 g/L	ALOGPS
logP	2.35	ALOGPS
logP	-0.5	ChemAxon
logS	-2.8	ALOGPS
pKa (Strongest Acidic)	0.83	ChemAxon
pKa (Strongest Basic)	4.95	ChemAxon
Physiological Charge	-4	ChemAxon
Hydrogen Acceptor Count	17	ChemAxon
Hydrogen Donor Count	9	ChemAxon
Polar Surface Area	363.63 Å²	ChemAxon
Rotatable Bond Count	34	ChemAxon
Refractivity	236.65 m³·mol⁻¹	ChemAxon
Polarizability	100.19 Å³	ChemAxon
Number of Rings	3	ChemAxon
Bioavailability	0	ChemAxon
Rule of Five	Yes	ChemAxon
Ghose Filter	Yes	ChemAxon
Veber's Rule	Yes	ChemAxon
MDDR-like Rule	Yes	ChemAxon

Biological Properties

Cellular Locations:

Cytoplasm

Reactions:

Adenosine triphosphate + Coenzyme A + Hydrogen ion + Palmitic acid > Adenosine monophosphate + Hydrogen ion + Palmityl-CoA + Pyrophosphate
3-Oxooctadecanoyl-CoA + Coenzyme A <> Acetyl-CoA + Palmityl-CoA
FAD + Palmityl-CoA <> FADH2 + (2E)-Hexadecenoyl-CoA
Water + Palmityl-CoA > Coenzyme A + Hydrogen ion + Palmitic acid
Adenosine triphosphate + Palmitic acid + Coenzyme A <> Adenosine monophosphate + Palmityl-CoA + Pyrophosphate
3-Oxotetradecanoyl-CoA + Coenzyme A > Acetyl-CoA + Palmityl-CoA
Palmityl-CoA + L-Carnitine <> L-Palmitoylcarnitine + Coenzyme A
Palmitic acid + Adenosine triphosphate + Coenzyme A > Palmityl-CoA + Adenosine monophosphate + Pyrophosphate
Palmityl-CoA + electron-transfer flavoprotein > (2E)-Hexadecenoyl-CoA + Reduced electron-transfer flavoprotein
Palmitic acid + Coenzyme A + Adenosine triphosphate > Adenosine monophosphate + Palmityl-CoA
Adenosine triphosphate + Coenzyme A + Hydrogen ion + Palmitic acid > Adenosine monophosphate + Palmityl-CoA + Pyrophosphate
Adenosine triphosphate + Coenzyme A + Hydrogen ion + Palmitic acid > Adenosine monophosphate + Palmityl-CoA + Pyrophosphate

SMPDB Pathways:

Fatty acid metabolism	PW000796
fatty acid oxidation (myristate)	PW001021
fatty acid oxidation (palmitate)	PW001023

KEGG Pathways:

Biosynthesis of unsaturated fatty acids ec01040
Fatty acid metabolism ec00071
Sphingolipid metabolism ec00600

EcoCyc Pathways:

Not Available

Concentrations

Not Available

Spectra

Spectra:

Spectrum Type	Description	Splash Key
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Positive	splash10-000i-2902100202-8995491c4408cb9cd2dd	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Positive	splash10-000i-0923300000-25204cd16c15043e7553	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Positive	splash10-000i-1900100100-10cdb45f6d139ab32fe0	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Negative	splash10-0fa9-9882342503-dc9f6ae4b03147f90b41	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Negative	splash10-0040-3921201001-8e28a440bd4fa5cf4e70	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Negative	splash10-057i-6900000000-e25d7582c34ed6bb66cf	View in MoNA
MS	Mass Spectrum (Electron Ionization)	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer

References

References:

Bajaj M, Suraamornkul S, Romanelli A, Cline GW, Mandarino LJ, Shulman GI, DeFronzo RA: Effect of a sustained reduction in plasma free fatty acid concentration on intramuscular long-chain fatty Acyl-CoAs and insulin action in type 2 diabetic patients. Diabetes. 2005 Nov;54(11):3148-53. Pubmed: 16249438
Bakken AM, Farstad M: Identical subcellular distribution of palmitoyl-CoA and arachidonoyl-CoA synthetase activities in human blood platelets. Biochem J. 1989 Jul 1;261(1):71-6. Pubmed: 2528345
Berge RK, Hagen LE, Farstad M: Isolation of palmitoyl-CoA hydrolases from human blood platelets. Biochem J. 1981 Dec 1;199(3):639-47. Pubmed: 6122441
Carroll JE, McGuire BS, Hall CL: Fatty acyl-CoA dehydrogenase enzymes in human skeletal muscle. Clin Chim Acta. 1986 Dec 30;161(3):327-33. Pubmed: 3802539
Casteels M, Schepers L, Parmentier G, Eyssen HJ, Mannaerts GP: Activation and peroxisomal beta-oxidation of fatty acids and bile acid intermediates in liver from Bombina orientalis and from the rat. Comp Biochem Physiol B. 1989;92(1):129-32. Pubmed: 2706931
Fukao T, Watanabe H, Orii K, Takahashi Y, Hirano A, Kondo T, Yamaguchi S, Aoyama T, Kondo N: Myopathic form of very-long chain acyl-coa dehydrogenase deficiency: evidence for temperature-sensitive mild mutations in both mutant alleles in a Japanese girl. Pediatr Res. 2001 Feb;49(2):227-31. Pubmed: 11158518
Gohil K, Jones DA, Edwards RH: Fatty acid oxidation in mitochondria from needle biopsy samples of human skeletal muscle. Clin Sci (Lond). 1984 Feb;66(2):173-8. Pubmed: 6319070
Haughey NJ, Cutler RG, Tamara A, McArthur JC, Vargas DL, Pardo CA, Turchan J, Nath A, Mattson MP: Perturbation of sphingolipid metabolism and ceramide production in HIV-dementia. Ann Neurol. 2004 Feb;55(2):257-67. Pubmed: 14755730
Holloway GP, Bezaire V, Heigenhauser GJ, Tandon NN, Glatz JF, Luiken JJ, Bonen A, Spriet LL: Mitochondrial long chain fatty acid oxidation, fatty acid translocase/CD36 content and carnitine palmitoyltransferase I activity in human skeletal muscle during aerobic exercise. J Physiol. 2006 Feb 15;571(Pt 1):201-10. Epub 2005 Dec 15. Pubmed: 16357012
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
Tonsgard JH, Stephens JK, Rhead WJ, Penn D, Horwitz AL, Kirschner BS, Whitington PF, Berger S, Tripp ME: Defect in fatty acid oxidation: laboratory and pathologic findings in a patient. Pediatr Neurol. 1991 Mar-Apr;7(2):125-30. Pubmed: 2059253
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
Wanders RJ, van Roermund CW, de Vries CT, van den Bosch H, Schrakamp G, Tager JM, Schram AW, Schutgens RB: Peroxisomal beta-oxidation of palmitoyl-CoA in human liver homogenates and its deficiency in the cerebro-hepato-renal (Zellweger) syndrome. Clin Chim Acta. 1986 Aug 30;159(1):1-10. Pubmed: 2944672

Synthesis Reference:

Not Available

Material Safety Data Sheet (MSDS)

Download (PDF)

Links

External Links:

Resource	Link
CHEBI ID	15525
HMDB ID	HMDB01338
Pubchem Compound ID	986
Kegg ID	C00154
ChemSpider ID	14902
Wikipedia	palmitoyl CoA
BioCyc ID	PALMITYL-COA
EcoCyc ID	PALMITYL-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. 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

4. 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

5. 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

6. 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

Palmityl-CoA (ECMDB01338) (M2MDB000343)

Structure for #<Compound:0xb05ec670>

Enzymes

Reactions

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