P. aeruginosa Metabolome Database: (2E)-Hexadecenoyl-CoA (PAMDB000541)

Identification Taxonomy Physical Properties Biological Properties Spectra Concentrations Links References Enzymes Transporters

Proteins (3280)

Record Information

Version

1.0

Update Date

1/22/2018 11:54:54 AM

Metabolite ID

PAMDB000541

Identification

Name:

(2E)-Hexadecenoyl-CoA

Description:

(2E)-Hexadecenoyl-CoA is an intermediate in fatty acid metabolism, the substrate of the enzyme enoyl-CoA hydratase [EC:4.2.1.17]. It is also the substrate of the enzyme trans-2-enoyl-CoA reductase [EC:1.3.1.38], in fatty acid elongation. (PMID: 1278159, KEGG)

Structure

🔍MOL SDF PDB SMILES InChI View Structure

Synonyms:

(2E)-Hexadecenoyl-CoA
(2E)-Hexadecenoyl-Coenzyme A
Trans-2-Hexadecenoyl-CoA
Trans-2-Hexadecenoyl-Coenzyme A

Chemical Formula:

C₃₇H₆₀N₇O₁₇P₃S

Average Molecular Weight:

999.895

Monoisotopic Molecular Weight:

999.297923755

InChI Key:

JUPAQFRKPHPXLD-MSHHSVQMSA-J

InChI:

InChI=1S/C37H64N7O17P3S/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/h16-17,24-26,30-32,36,47-48H,4-15,18-23H2,1-3H3,(H,39,45)(H,40,49)(H,53,54)(H,55,56)(H2,38,41,42)(H2,50,51,52)/p-4/b17-16+/t26-,30-,31-,32+,36-/m1/s1

CAS number:

4460-95-1

IUPAC Name:

(3R)-3-{[2-({2-[(2E)-hexadec-2-enoylsulfanyl]ethyl}carbamoyl)ethyl]carbamoyl}-3-hydroxy-2,2-dimethylpropyl ({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonatooxy)oxolan-2-yl]methyl phosphonato}oxy)phosphonate

Traditional IUPAC Name:

(E)-hexadec-2-enoyl-coa(4-)

SMILES:

CCCCCCCCCCCCC\C=C\C(=O)SCCNC(=O)CCNC(=O)[C@H](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

Taxonomy Description

This compound belongs to the class of organic compounds known as long-chain 2-enoyl coas. These are organic compounds containing a coenzyme A substructure linked to a long-chain 2-enoyl 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 2-enoyl CoAs

Alternative Parents

Substituents

Coenzyme a or derivatives
Purine ribonucleoside diphosphate
N-glycosyl compound
Glycosyl compound
Organic pyrophosphate
Monosaccharide phosphate
6-aminopurine
Purine
Imidazopyrimidine
Monoalkyl phosphate
Aminopyrimidine
Imidolactam
Alkyl phosphate
Pyrimidine
Primary aromatic amine
Phosphoric acid ester
Organic phosphoric acid derivative
Organic phosphate
N-substituted imidazole
Monosaccharide
Heteroaromatic compound
Oxolane
Imidazole
Azole
Thiocarboxylic acid ester
Secondary alcohol
Oxacycle
Azacycle
Organoheterocyclic compound
Sulfenyl compound
Thioether
Thiocarboxylic acid or derivatives
Carboxylic acid derivative
Carboximidic acid derivative
Carboximidic acid
Hydrocarbon derivative
Primary amine
Organosulfur compound
Organooxygen compound
Organonitrogen compound
Amine
Alcohol
Organic anion
Aromatic heteropolycyclic compound

Molecular Framework

Aromatic heteropolycyclic compounds

External Descriptors

monounsaturated fatty acyl-CoA(4-) (CHEBI:61526 )

Physical Properties

State:

Solid

Charge:

-4

Melting point:

Not Available

Experimental Properties:

Property	Value	Source
LogP:	2.319	PhysProp

Predicted Properties

Property	Value	Source
Water Solubility	1.22 mg/mL	ALOGPS
logP	3.34	ALOGPS
logP	-0.26	ChemAxon
logS	-2.9	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	5	ChemAxon
Polar Surface Area	374.95 Å²	ChemAxon
Rotatable Bond Count	33	ChemAxon
Refractivity	233.25 m³·mol^-1	ChemAxon
Polarizability	98.77 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:

(S)-3-Hydroxyhexadecanoyl-CoA <> Water + (2E)-Hexadecenoyl-CoA
FAD + Palmityl-CoA <> FADH2 + (2E)-Hexadecenoyl-CoA
Palmityl-CoA + electron-transfer flavoprotein > (2E)-Hexadecenoyl-CoA + Reduced electron-transfer flavoprotein
(S)-3-Hydroxyhexadecanoyl-CoA > (2E)-Hexadecenoyl-CoA

Pathways:

Fatty acid metabolism pae00071

Spectra

Spectra:

Spectrum Type	Description	Splash Key
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Positive	splash10-0zfr-9000000100-a1fa399e8b9a0f5a7be2	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Positive	splash10-0btc-9105020007-451c96f9724068202e5a	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Positive	splash10-01ox-8915200100-0a7f3c9c09ea57c0b387	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Negative	splash10-0002-3000000009-b59c42d14785cf69a6d0	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Negative	splash10-0a4j-6090200005-6be90b350179fc9c49c0	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Negative	splash10-01si-9700110000-b7c4f7cab1d1a272cd4b	View in MoNA

References

References:

Hinsch, W., Klages, C., Seubert, W. (1976). "On the mechanism of malonyl-CoA-independent fatty-acid synthesis. Different properties of the mitochondrial chain elongation and enoylCoA reductase in various tissues." Eur J Biochem 64:45-55. Pubmed: 1278159
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

Synthesis Reference:

Al-Arif, Adhid; Blecher, Melvin. Chemical synthesis of carnitine and coenzyme A esters of the b-substituted intermediates of hexadecanoic acid metabolism. Biochimica et Biophysica Acta, Lipids and Lipid Metabolism (1971), 248(3), 416-29.

Material Safety Data Sheet (MSDS)

Not Available

Links

External Links:

Resource	Link
CHEBI ID	28935
HMDB ID	HMDB03945
Pubchem Compound ID	5280766
Kegg ID	C05272
ChemSpider ID	26332261
Wikipedia ID	Not Available
BioCyc ID	CPD0-2117
EcoCyc ID	CPD0-2117

Enzymes

Protein Details

• Fatty acid oxidation complex subunit alpha

General function:: Involved in 3-hydroxyacyl-CoA dehydrogenase activity
Specific function:: Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities. Involved in the aerobic and anaerobic degradation of long-chain fatty acids
Gene Name:: fadB
Locus Tag:: PA3014
Molecular weight:: 77 kDa

Reactions

(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH.
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O.
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.

Protein Details

• 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
Locus Tag:: PA3299
Molecular weight:: 61.7 kDa

Reactions

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Protein Details

• Acyl-coenzyme A dehydrogenase

General function:: Involved in acyl-CoA dehydrogenase activity
Specific function:: Catalyzes the dehydrogenation of acyl-CoA
Gene Name:: fadE
Locus Tag:: PA2815
Molecular weight:: 88.8 kDa

Reactions

An acyl-CoA + FAD = a dehydrogenated acyl-CoA + FADH(2).

Protein Details

• 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
Locus Tag:: PA3942
Molecular weight:: 32.9 kDa

(2E)-Hexadecenoyl-CoA (PAMDB000541)

Structure for (2E)-Hexadecenoyl-CoA (PAMDB000541)

Enzymes

Reactions

Reactions

Reactions