COENZYME A

CoA

CAS Number: 85-61-0

Chemical formula: C21H36N7O16P3S
Molar mass: 767.535

Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for Coenzyme A role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. 
All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use Coenzyme A (or a thioester) as a substrate. 
In humans, CoA biosynthesis requires cysteine, pantothenate (vitamin B5), and adenosine triphosphate (ATP).

In Coenzyme A acetyl form, coenzyme A is a highly versatile molecule, serving metabolic functions in both the anabolic and catabolic pathways. 
Acetyl-CoA is utilised in the post-translational regulation and allosteric regulation of pyruvate dehydrogenase and carboxylase to maintain and support the partition of pyruvate synthesis and degradation.

Coenzyme A is so called because Coenzyme A was identified by Lipmann et al. (1947) as the heat-stable cofactor for acetylation reactions, the A standing for acetylation. 
The active part of the molecule is the terminal thiol group, which is covalently linked via a thioester bond to acyl groups such as acetate, or longer chain fatty acids. 

The CoA derivative is more soluble in the aqueous environment of the cell and is said to be activated because the ΔG of hydrolysis of the thioester linkage is large and negative (e.g. − 31.5 kJ mol− 1 for acetyl CoA). 
This then facilitates the formation of covalent bonds, such as citrate from acetyl CoA and oxaloacetate in the Krebs’ cycle. 

CoA is involved in innumerable reactions of central metabolism (e.g. fatty acid oxidation, and biosynthesis of glycerolipids and sterols) as well as secondary metabolic pathways, including those for polyketides, non-ribosomal protein synthesis, flavonoids, and lignin. 
In Escherichia coli, Coenzyme A has been estimated that approximately 100 enzymes (over 4% of the total) use either CoA or a CoA ester as substrate. 

ACPs have a much more restricted, although equally important, role in fatty acid synthesis, and in E. coli, ACP is the most abundant soluble protein constituting about 0.25% of the total soluble protein. 
Again the acyl groups are attached via a thioester link to the terminal thiol. 

Transthioesterification is readily achieved and this reactivity is central to the chemistry of these thioesters. 
The pKa of the alpha proton is also reduced by thioesterification, enabling Claisen ester condensation chemistry to occur readily in pathways of fatty acid biosynthesis.

Coenzyme A (CoA, CoASH or HSCoA) is the key cofactor in first step of the TCA cycle, responsible for transferring the acetyl group from pyruvate oxidation to oxaloacetate yielding citrate.

Coenzyme A is also a critical cofactor in fatty acid metabolism. 
Coenzyme A carries fatty acids through the catabolic/oxidation process in the mitochondria and transfers acetyl groups during the elongation process of fatty acid synthesis in the cytosol.

The acetyl moiety of acetylCoA is bound by a high-energy bond (free energy 34.3 kJ/mol) to the -SH group of Coenzyme A. 
Coenzyme A is also a precursor to, steroids and other naturally occurring compounds, such as terpenes and acetogenins present in plants.

In the transfer reaction by Acetyl CoA of the C2 acetyl fragment, either the carboxyl group or the methyl group may react (electrophilic vs. nucleophilic reaction, respectively).

AcetylCoA is prepared enzymatically by reacting Coenzyme A with Acetyl Phosphate and Phosphotransacetylase. 
The product is purified by ion exchange chromatography. 

Several methods of preparation and methods for the determination of Acetyl CoA and other CoA derivatives have been described in the literature.
Coenzyme A is synthesized in vivo from pantothenate, cysteine, and adenosine. 
Pantothenate is phosphorylated, joined with cysteine, decarboxylated, joined with adenosine and phosphorylated again to the 3’ ribose position to yield Coenzyme A. 

Coenzyme A (CoA) is an essential metabolic cofactor synthesized from cysteine, pantothenate, and ATP. 
CoA plays important roles in many metabolic pathways, including the tricarboxylic acid cycle, and the synthesis and oxidation of fatty acids. 

One of the main functions of CoA is the carrying and transfer of acyl groups. 
Acylated deriviates, for example acetyl-CoA, are critical intermediates in many metabolic reactions. 
CoA levels can be altered during starvation, and in conditions such as cancer, diabetes, and alcoholism.

Coenzyme A can bind acetate (Acetyl-CoA) or other carboxylic acids in an energy-rich binding. 
Coenzyme A is cofactor of many enzyme-catalysed acetylations, e. g. in the citrate cycle (Krebs cycle). 
For improving the sensitivity of the luciferase assay, CoA is added to the assay buffer at a concentration of 270 μM.

Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme notable for Coenzyme A role in the synthesis and oxidization of fatty acids and the oxidation of pyruvate in the citric acid cycle. 
Coenzyme A is adapted from beta-mercaptoethylamine, panthothenate, and adenosine triphosphate. 

Coenzyme A is also a parent compound for other transformation products, including but not limited to, phenylglyoxylyl-CoA, tetracosanoyl-CoA, and 6-hydroxyhex-3-enoyl-CoA. 
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, Coenzyme A 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 the mitochondria. 
A molecule of coenzyme A carrying an acetyl group is also referred to as acetyl-CoA. 

When Coenzyme A is not attached to an acyl group, Coenzyme A 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 proteins and formyltetrahydrofolate dehydrogenase. 

Acetyl-CoA is an important molecule itself. 
Coenzyme A is the precursor to HMG CoA which is a vital component in cholesterol and ketone synthesis. 

Furthermore, Coenzyme A contributes an acetyl group to choline to produce acetylcholine in a reaction catalysed by choline acetyltransferase. 
Coenzyme A main task is conveying the carbon atoms within the acetyl group to the citric acid cycle to be oxidized for energy production.

Coenzyme A, also known as CoA or coenzyme A-SH, belongs to the class of organic compounds known as coenzyme a and derivatives. 
These are derivative of vitamin B5 containing a 4'-phosphopantetheine moiety attached to a diphospho-adenosine. 

Coenzyme A is a strong basic compound (based on its pKa). 
Coenzyme A exists in all living species, ranging from bacteria to humans.

Coenzyme A (CoA) is a ubiquitous essential cofactor that plays a central role in the metabolism of carboxylic acids, including short- and long-chain fatty acids, as well as carbohydrate and protein. 
In the metabolic pathway of lipid, CoA participates in fatty acid β-oxidation, promoting triglyceride (TG) catabolism. 

Coenzyme A functions as an acyl group carrier and assists in transferring fatty acids from the cytoplasm to mitochondria. 
All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use Coenzyme A (or a thioester, such as acetyl-CoA) as a substrate. 

Coenzyme A is the most active metabolic enzyme in the human body. 
Coenzyme A is used as a supplement for the hypothetical treatment of acne.

Coenzyme A (CoA) is a derivative of vitamin B5 and cysteine. 
One of CoA’s largest roles comes in the form of acetyl-CoA. 

Acetyl-CoA is produced when CoA is linked to an acetyl group through a thioester bond. 
Acetyl-CoA plays a key role in intermediate metabolism in organisms ranging from archaebacteria to mammals. 

Some of Coenzyme A major roles include being a precursor of anabolic reactions, regulation of enzymatic activity via allosteric interactions, and facilitation of acetyl transfer to proteins. 
Acetyltransferases (NATs) facilitate the transfer of an acetyl group from acetyl-CoA to the "-amino group on the N-terminal residue of a protein. 

This terminal acetylation greatly affects the stability and function of a protein. 
The abundance of acetyl-CoA in cellular compartments can change based on various physiological and/or pathological conditions. 

Research has shown that acetyl-CoA is involved in some cell regulation processes via Coenzyme A ability to control the balance between anabolic and catabolic reactions. 
Several pharmaceutical agents have been and continue to be developed to influence acetyl-CoA metabolism.

Biosynthesis of Coenzyme A:
Coenzyme A is naturally synthesized from pantothenate (vitamin B5), which is found in food such as meat, vegetables, cereal grains, legumes, eggs, and milk.
In humans and most living organisms, pantothenate is an essential vitamin that has a variety of functions.

In some plants and bacteria, including Escherichia coli, pantothenate can be synthesised de novo and is therefore not considered essential. 
These bacteria synthesize pantothenate from the amino acid aspartate and a metabolite in valine biosynthesis.

In all living organisms, coenzyme A is synthesized in a five-step process that requires four molecules of ATP, pantothenate and cysteine:
Pantothenate (vitamin B5) is phosphorylated to 4′-phosphopantothenate by the enzyme pantothenate kinase (PanK; CoaA; CoaX). 
This is the committed step in CoA biosynthesis and requires ATP.

A cysteine is added to 4′-phosphopantothenate by the enzyme phosphopantothenoylcysteine synthetase (PPCS; CoaB) to form 4'-phospho-N-pantothenoylcysteine (PPC). 
This step is coupled with ATP hydrolysis.

PPC is decarboxylated to 4′-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (PPC-DC; CoaC)

4′-phosphopantetheine is adenylated (or more properly, AMPylated) to form dephospho-CoA by the enzyme phosphopantetheine adenylyl transferase (COASY; PPAT; CoaD)

Finally, dephospho-CoA is phosphorylated to coenzyme A by the enzyme dephosphocoenzyme A kinase (COASY, DPCK; CoaE). 
This final step requires ATP.

Enzyme nomenclature abbreviations in parentheses represent mammalian, other eukaryotic, and prokaryotic enzymes respectively. 
In mammals steps 4 and 5 are catalyzed by a bifunctional enzyme called COASY.

This pathway is regulated by product inhibition. 
CoA is a competitive inhibitor for Pantothenate Kinase, which normally binds ATP.
Coenzyme A, three ADP, one monophosphate, and one diphosphate are harvested from biosynthesis.

Coenzyme A can be synthesized through alternate routes when intracellular coenzyme A level are reduced and the de novo pathway is impaired.
In these pathways, coenzyme A needs to be provided from an external source, such as food, in order to produce 4′-phosphopantetheine. 

Ectonucleotide pyrophosphates (ENPP) degrade coenzyme A to 4′-phosphopantetheine, a stable molecule in organisms. 
Acyl carrier proteins (ACP) (such as ACP synthase and ACP degradation) are also used to produce 4′-phosphopantetheine. 
This pathway allows for 4′-phosphopantetheine to be replenished in the cell and allows for the conversion to coenzyme A through enzymes, PPAT and PPCK.

Commercial production of Coenzyme A:
Coenzyme A is produced commercially via extraction from yeast, however this is an inefficient process (yields approximately 25 mg/kg) resulting in an expensive product. 
Various ways of producing CoA synthetically, or semi-synthetically have been investigated although none are currently operating at an industrial scale.

Pharmacology and Biochemistry of Coenzyme A:

Human Metabolite Information:

Tissue Locations:
Adipose Tissue
Fibroblasts
Skeletal Muscle

Cellular Locations:
Endoplasmic reticulum
Golgi apparatus
Lysosome
Mitochondria
Nucleus
Peroxisome

Metabolite Pathways:
2-aminoadipic 2-oxoadipic aciduria
2-Hydroxyglutric Aciduria (D And L Form)
2-ketoglutarate dehydrogenase complex deficiency
2-Methyl-3-Hydroxybutryl CoA Dehydrogenase Deficiency
27-Hydroxylase Deficiency
3-Hydroxy-3-Methylglutaryl-CoA Lyase Deficiency
3-hydroxyisobutyric acid dehydrogenase deficiency
3-hydroxyisobutyric aciduria
3-Methylcrotonyl Coa Carboxylase Deficiency Type I
3-Methylglutaconic Aciduria Type I

Function of Coenzyme A:

Fatty acid synthesis:
Since coenzyme A is, in chemical terms, a thiol, Coenzyme A can react with carboxylic acids to form thioesters, thus functioning as an acyl group carrier. 
Coenzyme A assists in transferring fatty acids from the cytoplasm to mitochondria. 

A molecule of coenzyme A carrying an acyl group is also referred to as acyl-CoA. 
When Coenzyme A is not attached to an acyl group, Coenzyme A is usually referred to as 'CoASH' or 'HSCoA'. 
This process facilitates the production of fatty acids in cells, which are essential in cell membrane structure.

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.

Energy production:
Coenzyme A is one of five crucial coenzymes that are necessary in the reaction mechanism of the citric acid cycle. 
Coenzyme A acetyl-coenzyme A form is the primary input in the citric acid cycle and is obtained from glycolysis, amino acid metabolism, and fatty acid beta oxidation. 
This process is the body's primary catabolic pathway and is essential in breaking down the building blocks of the cell such as carbohydrates, amino acids, and lipids.

Regulation:
When there is excess glucose, coenzyme A is used in the cytosol for synthesis of fatty acids.
This process is implemented by regulation of acetyl-CoA carboxylase, which catalyzes the committed step in fatty acid synthesis. 
Insulin stimulates acetyl-CoA carboxylase, while epinephrine and glucagon inhibit Coenzyme A activity.

During cell starvation, coenzyme A is synthesized and transports fatty acids in the cytosol to the mitochondria. 
Here, acetyl-CoA is generated for oxidation and energy production.
In the citric acid cycle, coenzyme A works as an allosteric regulator in the stimulation of the enzyme pyruvate dehydrogenase.

New research has found that protein CoAlation plays an important role in regulation of the oxidative stress response. 
Protein CoAlation plays a similar role to S-glutathionylation in the cell, and prevents the irreversible oxidation of the thiol group in cysteine on the surface of cellular proteins, while also directly regulating enzymatic activity in response to oxidative or metabolic stress.

Uses of Coenzyme A:
As essential cofactor in acetyl transfer reactions found in mammalian cells and many microorganisms.
Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, notable for Coenzyme A role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle.

Use in biological research of Coenzyme A:
Coenzyme A is available from various chemical suppliers as the free acid and lithium or sodium salts. 
The free acid of coenzyme A is detectably unstable, with around 5% degradation observed after 6 months when stored at −20 °C, and near complete degradation after 1 month at 37 °C.

The lithium and sodium salts of CoA are more stable, with negligible degradation noted over several months at various temperatures.
Aqueous solutions of coenzyme A are unstable above pH 8, with 31% of activity lost after 24 hours at 25 °C and pH 8. 

CoA stock solutions are relatively stable when frozen at pH 2–6. 
The major route of CoA activity loss is likely the air oxidation of CoA to CoA disulfides. 

CoA mixed disulfides, such as CoA-S–S-glutathione, are commonly noted contaminants in commercial preparations of CoA.
Free CoA can be regenerated from CoA disulfide and mixed CoA disulfides with reducing agents such as dithiothreitol or 2-mercaptoethanol.

Non-exhaustive list of coenzyme A-activated acyl groups:
Acetyl-CoA
fatty acyl-CoA (activated form of all fatty acids; only the CoA esters are substrates for important reactions such as mono-, di-, and triacylglycerol synthesis, carnitine palmitoyl transferase, and cholesterol esterification)
Propionyl-CoA
Butyryl-CoA
Myristoyl-CoA
Crotonyl-CoA
Acetoacetyl-CoA
Coumaroyl-CoA (used in flavonoid and stilbenoid biosynthesis)
Benzoyl-CoA
Phenylacetyl-CoA
Acyl derived from dicarboxylic acids
Malonyl-CoA (important in chain elongation in fatty acid biosynthesis and polyketide biosynthesis)
Succinyl-CoA (used in heme biosynthesis)
Hydroxymethylglutaryl-CoA (used in isoprenoid biosynthesis)
Pimelyl-CoA (used in biotin biosynthesis)

Discovery of structure of Coenzyme A:
Coenzyme A was identified by Fritz Lipmann in 1946, who also later gave Coenzyme A its name. 
Coenzyme A structure was determined during the early 1950s at the Lister Institute, London, together by Lipmann and other workers at Harvard Medical School and Massachusetts General Hospital.

Lipmann initially intended to study acetyl transfer in animals, and from these experiments he noticed a unique factor that was not present in enzyme extracts but was evident in all organs of the animals. 
He was able to isolate and purify the factor from pig liver and discovered that Coenzyme A function was related to a coenzyme that was active in choline acetylation.

Work with Beverly Guirard, Nathan Kaplan, and others determined that pantothenic acid was a central component of coenzyme A.
The coenzyme was named coenzyme A to stand for "activation of acetate". 
In 1953, Fritz Lipmann won the Nobel Prize in Physiology or Medicine "for his discovery of co-enzyme A and Coenzyme A importance for intermediary metabolism".

Discovery of Coenzyme A:
Coenzyme A (CoA) was discovered by Fritz Lipmann and his colleagues in the early 1950s. 
The coenzyme was first isolated from large quantities of pig liver extract as the factor required for the acetylation of sulfanilamide, the assay system used to track CoA during Coenzyme A purification. 

The discovery of CoA and the characterization and determination of Coenzyme A structure led Lipmann being awarded the 1953 Nobel prize in physiology or medicine. 
Lipmann's findings opened the door for the discovery of innumerable roles of CoA, most notably the discovery by Feodor Lynen that active acetate was acetyl-CoA, a key intermediate in the metabolism of carbon compounds by all organisms. 

In 1964, Lynen was awarded the Nobel prize in physiology or medicine for his discovery of acetyl-CoA and many of the metabolic systems that CoA functions. 
We now know that CoA plays a key role in carbohydrate, lipid, and amino acid metabolism.

Identifiers of Coenzyme A:
CAS Number:
85-61-0 (free acid)
55672-92-9 (sodium salt hydrate) 
18439-24-2 (lithium salt) 
ChEBI: CHEBI:15346
ChEMBL: ChEMBL1213327
ChemSpider: 6557
DrugBank: DB01992
ECHA InfoCard: 100.001.472
KEGG: C00010
MeSH: Coenzyme+A
PubChem CID: 6816
UNII: SAA04E81UX
InChI:
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 check
Key: RGJOEKWQDUBAIZ-DRCCLKDXSA-N check
InChI=1/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
Key: RGJOEKWQDUBAIZ-DRCCLKDXBU
SMILES: O=C(NCCS)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OC[C@H]3O[C@@H](n2cnc1c(ncnc12)N)[C@H](O)[C@@H]3OP(=O)(O)O

Properties of Coenzyme A:
Chemical formula: C21H36N7O16P3S
Molar mass: 767.535
UV-vis (λmax): 259.5 nm[1]
Absorbance: ε259 = 16.8 mM−1 cm−1 

Molecular Weight: 767.5
XLogP3: -5.8
Hydrogen Bond Donor Count: 10
Hydrogen Bond Acceptor Count: 21
Rotatable Bond Count: 18
Exact Mass: 767.11521025
Monoisotopic Mass: 767.11521025
Topological Polar Surface Area: 348 Ų
Heavy Atom Count: 48
Complexity: 1270    
Isotope Atom Count: 0
Defined Atom Stereocenter Count: 5
Undefined Atom Stereocenter Count: 0
Defined Bond Stereocenter Count: 0
Undefined Bond Stereocenter Count: 0
Covalently-Bonded Unit Count: 1
Compound Is Canonicalized: Yes

Names of Coenzyme A:

Systematic IUPAC name of Coenzyme A:
[(2R,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydro-2-furanyl]methyl 
(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 
dihydrogen diphosphate

Synonyms of Coenzyme A:
coenzyme A
CoASH
85-61-0
CoA-SH
Zeel
CoA
Depot-Zeel
HSCoA
Coenzym A
co-enzyme-A
Coenzyme ASH
UNII-SAA04E81UX
Phosphoteric T-C6
HS-CoA
COENZYME_A
SAA04E81UX
CHEBI:15346
3'-phosphoadenosine-(5')diphospho(4')pantatheine
Coenzyme A hydrate
[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[[3-oxo-3-(2-sulfanylethylamino)propyl]amino]butyl] hydrogen phosphate
143180-18-1
Co-A-SH
Lucina
Reduced CoA
[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R)-3-hydroxy-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate
3'-phosphoadenosine 5'-{3-[(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl] dihydrogen diphosphate}
Aluzime
Coalip
coenzymes A
S-propanoate
coenzyme-A
CoA hydrate
Koenzym A
S-propanoic acid
Thiol-CoA
S-propanoate CoA
S-propionate CoA
D-Coenzyme A
Coenzyme A-SH
Adenosine 5'-(trihydrogen diphosphate) 3'-(dihydrogen phosphate) P'-[(R)-3-hydroxy-4-[[3-[(2-mercaptoethyl)amino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutyl] ester
co-A
EINECS 201-619-0
S-propanoate Coenzyme A
S-propionate Coenzyme A
GTPL3044
CHEMBL1213327
SCHEMBL18180012
MCC2008
ZINC8551087
BDBM50367033
AKOS025310810
DB01992
HY-128851
CS-0100923
C00010
A904100
(((2R,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-4-hydroxy-2-(((hydroxy((hydroxy((R)-3-hydroxy-2,2-dimethyl-3-((2-((2-sulfanylethyl)carbamoyl)ethyl)carbamoyl)propoxy)phosphoryl)oxy)phosphoryl)oxy)methyl)oxolan-3-yl)oxy)phosphonic acid
[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl dihydrogen diphosphate (non-preferred name)
[(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
[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methyl [hydroxy-[(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[[3-oxo-3-(2-sulfanylethylamino)propyl]amino]butoxy]phosphoryl] hydrogen phosphate
9H-purin-6-amine,9-[5-O-[hydroxy[[hydroxy[[(3R)-3-hydroxy-4-[[3-[(2-mercaptoethyl)amino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutyl]oxy]phosphinyl]oxy]phosphinyl]-3-O-phosphono-beta-D-ribofuranosyl]-
Adenosine 5'-(trihydrogen diphosphate), 3'-(dihydrogen phosphate), P'-[3-hydroxy-4-[[3-[(2-mercaptoethyl)amino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutyl] ester, (R)-
[(2R,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydro-2-furanyl]methyl (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl dihydrogen dipho sphate [ACD/IUPAC Name]
[(2R,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydro-2-furanyl]methyl (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl dihydrogen diphosphate
[(2R,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydro-2-furanyl]methyl-(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyldihydrogendiphosp hat [German] [ACD/IUPAC Name]
201-619-0
85-61-0
Adenosine, 5'-O-[hydroxy[[hydroxy[(3R)-3-hydroxy-4-[[3-[(2-mercaptoethyl)amino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutoxy]phosphinyl]oxy]phosphinyl]-, 3'-(dihydrogen phosphate) [ACD/Index Name]
CoA
CoASH
Coenzym A
Coenzyme A
coenzyme-A
co-enzyme-A
Dihydrogénodiphosphate de [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tétrahydro-2-furanyl]méthyle et de (3R)-3-hydroxy-2,2-diméthyl-4-oxo-4-({3-oxo-3-[(2-sulfanyléthyl)amino]pr opyl}amino)butyle [French] [ACD/IUPAC Name]
HSCoA
HS-CoA
SAA04E81UX
[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R)-3-hydroxy-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate
[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R)-3-hydroxy-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)-2,2-dimethyl-4-oxobutyl dihydrogen diphosphateLucina
[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methyl [hydroxy-[(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[[3-oxo-3-(2-sulfanylethylamino)propyl]amino]butoxy]phosphoryl] hydrogen phosphate
[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[[3-oxo-3-(2-sulfanylethylamino)propyl]amino]butyl] hydrogen phosphate
143180-18-1 [RN]
18-CoA-18-oxo-dinor-LTB4
1VU
3'-phosphoadenosine 5'-{3-[(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl] dihydrogen diphosphate}
3'-phosphoadenosine-(5')diphospho(4')pantatheine
77809 [Beilstein]
9H-purin-6-amine,9-[5-O-[hydroxy[[hydroxy[[(3R)-3-hydroxy-4-[[3-[(2-mercaptoethyl)amino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutyl]oxy]phosphinyl]oxy]phosphinyl]-3-O-phosphono-β-D-ribofuranosyl]-
acetoacetyl-coenzyme a
Acetyl coenzyme A
ACO
Adenosine 5'-(trihydrogen diphosphate) 3'-(dihydrogen phosphate) P'-[(R)-3-hydroxy-4-[[3-[(2-mercaptoethyl)amino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutyl] ester
Adenosine 5'-(trihydrogen diphosphate), 3'-(dihydrogen phosphate), P'-[3-hydroxy-4-[[3-[(2-mercaptoethyl)amino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutyl] ester, (R)-
Aluzime
CAA
CAO
co-A
Coali
Coalip
CoA-SH
Co-A-SH
Coenzyme A|coenzyme A
Coenzyme ASH
co-enzyme-A|CoA
Koenzym A
Lucina
Malonyl-coenzyme A
MFCD06795839
MLC
pCoenzyme ASH
Phosphoteric T-C6
Propionyl coenzyme A
Thiol-CoA
UNII:SAA04E81UX
UNII-SAA04E81UX