Coenzyme A

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Coenzyme A
Coenzym A.svg
Coenzyme-A-3D-balls.png
Coenzyme-A-3D-vdW.png
Names
Systematic 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
Identifiers
3D model (JSmol)
ChEBI
ChEMBL
ChemSpider
DrugBank
ECHA InfoCard 100.001.472 OOjs UI icon edit-ltr-progressive.svg
KEGG
MeSH Coenzyme+A
PubChem CID
UNII
  • 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 Yes check.svgY
    Key: RGJOEKWQDUBAIZ-DRCCLKDXSA-N Yes check.svgY
  • 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
  • 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
C21H36N7O16P3S
Molar mass 767.535
UV-vis (λmax)259.5 nm [1]
Absorbance ε259 = 16.8 mM−1 cm−1 [1]
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
X mark.svgN  verify  (what is  Yes check.svgYX mark.svgN ?)

Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its 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 it (or a thioester) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenate (vitamin B5), and adenosine triphosphate (ATP). [2]

Contents

In its 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. [3]

Discovery of structure

Structure of coenzyme A: 1: 3'-phosphoadenosine. 2: diphosphate, organophosphate anhydride. 3: pantoic acid. 4: b-alanine. 5: cysteamine. Coenzym A beschriftet.svg
Structure of coenzyme A: 1: 3′-phosphoadenosine. 2: diphosphate, organophosphate anhydride. 3: pantoic acid. 4: β-alanine. 5: cysteamine.

Coenzyme A was identified by Fritz Lipmann in 1946, [4] who also later gave it its name. Its 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. [5] 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 its function was related to a coenzyme that was active in choline acetylation. [6] Work with Beverly Guirard, Nathan Kaplan, and others determined that pantothenic acid was a central component of coenzyme A. [7] [8] 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 its importance for intermediary metabolism". [6] [9]

Biosynthesis

Coenzyme A is naturally synthesized from pantothenate (vitamin B5), which is found in food such as meat, vegetables, cereal grains, legumes, eggs, and milk. [10] In humans and most living organisms, pantothenate is an essential vitamin that has a variety of functions. [11]  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. [12]

In all living organisms, coenzyme A is synthesized in a five-step process that requires four molecules of ATP, pantothenate and cysteine [13] (see figure):

Details of the biosynthetic pathway of CoA synthesis from pantothenic acid. CoA Biosynthetic Pathway.png
Details of the biosynthetic pathway of CoA synthesis from pantothenic acid.
  1. 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. [12]
  2. 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. [12]
  3. PPC is decarboxylated to 4′-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (PPC-DC; CoaC)
  4. 4′-phosphopantetheine is adenylated (or more properly, AMPylated) to form dephospho-CoA by the enzyme phosphopantetheine adenylyl transferase (COASY; PPAT; CoaD)
  5. Finally, dephospho-CoA is phosphorylated to coenzyme A by the enzyme dephosphocoenzyme A kinase (COASY, DPCK; CoaE). This final step requires ATP. [12]

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. [14] This pathway is regulated by product inhibition. CoA is a competitive inhibitor for Pantothenate Kinase, which normally binds ATP. [12] Coenzyme A, three ADP, one monophosphate, and one diphosphate are harvested from biosynthesis. [13]

Coenzyme A can be synthesized through alternate routes when intracellular coenzyme A level are reduced and the de novo pathway is impaired. [15] 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. [16]

A 2024 article[ citation needed ] detailed a plausible chemical synthesis mechanism for the pantetheine component (the main functional part) of coenzyme A in a primordial prebiotic world.

Commercial production

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. [17]

Function

Fatty acid synthesis

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. It 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 it is not attached to an acyl group, it 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. [18] [19]

Some of the sources that CoA comes from and uses in the cell. CoA Sources and Uses.png
Some of the sources that CoA comes from and uses in the cell.

Energy production

Coenzyme A is one of five crucial coenzymes that are necessary in the reaction mechanism of the citric acid cycle. Its 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. [20]

Regulation

When there is excess glucose, coenzyme A is used in the cytosol for synthesis of fatty acids. [21] 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 its activity. [22]

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. [21] In the citric acid cycle, coenzyme A works as an allosteric regulator in the stimulation of the enzyme pyruvate dehydrogenase.

Antioxidant function and regulation

Discovery of the novel antioxidant function of coenzyme A highlights its protective role during cellular stress. Mammalian and Bacterial cells subjected to oxidative and metabolic stress show significant increase in the covalent modification of protein cysteine residues by coenzyme A. [23] [24] This reversible modification is termed protein CoAlation (Protein-S-SCoA), which plays a similar role to protein S-glutathionylation by preventing the irreversible oxidation of the thiol group of cysteine residues.

Using anti-coenzyme A antibody [25] and liquid chromatography tandem mass spectrometry (LC-MS/MS) methodologies, more than 2,000 CoAlated proteins were identified from stressed mammalian and bacterial cells. [26] The majority of these proteins are involved in cellular metabolism and stress response. [26] Different research studies have focused on deciphering the coenzyme A-mediated regulation of proteins. Upon protein CoAlation, inhibition of the catalytic activity of different proteins (e.g. metastasis suppressor NME1, peroxiredoxin 5, GAPDH, among others) is reported. [27] [28] [24] [29] To restore the protein's activity, antioxidant enzymes that reduce the disulfide bond between coenzyme A and the protein cysteine residue play an important role. This process is termed protein deCoAlation. So far, two bacterial proteins, Thioredoxin A and Thioredoxin-like protein (YtpP), are shown to deCoAlate proteins. [30]

Use in biological research

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, [1] and near complete degradation after 1 month at 37 °C. [31] The lithium and sodium salts of CoA are more stable, with negligible degradation noted over several months at various temperatures. [32] 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. [1] 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

Related Research Articles

<span class="mw-page-title-main">Metabolism</span> Set of chemical reactions in organisms

Metabolism is the set of life-sustaining chemical reactions in organisms. The three main functions of metabolism are: the conversion of the energy in food to energy available to run cellular processes; the conversion of food to building blocks of proteins, lipids, nucleic acids, and some carbohydrates; and the elimination of metabolic wastes. These enzyme-catalyzed reactions allow organisms to grow and reproduce, maintain their structures, and respond to their environments. The word metabolism can also refer to the sum of all chemical reactions that occur in living organisms, including digestion and the transportation of substances into and between different cells, in which case the above described set of reactions within the cells is called intermediary metabolism.

<span class="mw-page-title-main">Pantothenic acid</span> Chemical compound

Pantothenic acid (vitamin B5) is a B vitamin and an essential nutrient. All animals need pantothenic acid in order to synthesize coenzyme A (CoA), which is essential for cellular energy production and for the synthesis and degradation of proteins, carbohydrates, and fats.

<span class="mw-page-title-main">Glutathione</span> Ubiquitous antioxidant compound in living organisms

Glutathione is an organic compound with the chemical formula HOCOCH(NH2)CH2CH2CONHCH(CH2SH)CONHCH2COOH. It is an antioxidant in plants, animals, fungi, and some bacteria and archaea. Glutathione is capable of preventing damage to important cellular components caused by sources such as reactive oxygen species, free radicals, peroxides, lipid peroxides, and heavy metals. It is a tripeptide with a gamma peptide linkage between the carboxyl group of the glutamate side chain and cysteine. The carboxyl group of the cysteine residue is attached by normal peptide linkage to glycine.

<span class="mw-page-title-main">Lipoic acid</span> Chemical compound

Lipoic acid (LA), also known as α-lipoic acid, alpha-lipoic acid (ALA) and thioctic acid, is an organosulfur compound derived from caprylic acid (octanoic acid). ALA, which is made in animals normally, is essential for aerobic metabolism. It is also available as a dietary supplement or pharmaceutical drug in some countries. Lipoate is the conjugate base of lipoic acid, and the most prevalent form of LA under physiological conditions. Only the (R)-(+)-enantiomer (RLA) exists in nature. RLA is an essential cofactor of many processes.

<span class="mw-page-title-main">Acetyl-CoA</span> Chemical compound

Acetyl-CoA is a molecule that participates in many biochemical reactions in protein, carbohydrate and lipid metabolism. Its main function is to deliver the acetyl group to the citric acid cycle to be oxidized for energy production.

<span class="mw-page-title-main">Carnitine</span> Amino acid active in mitochondria

Carnitine is a quaternary ammonium compound involved in metabolism in most mammals, plants, and some bacteria. In support of energy metabolism, carnitine transports long-chain fatty acids from the cytosol into mitochondria to be oxidized for free energy production, and also participates in removing products of metabolism from cells. Given its key metabolic roles, carnitine is concentrated in tissues like skeletal and cardiac muscle that metabolize fatty acids as an energy source. Generally individuals, including strict vegetarians, synthesize enough L-carnitine in vivo.

Fatty acid metabolism consists of various metabolic processes involving or closely related to fatty acids, a family of molecules classified within the lipid macronutrient category. These processes can mainly be divided into (1) catabolic processes that generate energy and (2) anabolic processes where they serve as building blocks for other compounds.

In biochemistry and metabolism, beta oxidation (also β-oxidation) is the catabolic process by which fatty acid molecules are broken down in the cytosol in prokaryotes and in the mitochondria in eukaryotes to generate acetyl-CoA. Acetyl-CoA enters the citric acid cycle, generating NADH and FADH2, which are electron carriers used in the electron transport chain. It is named as such because the beta carbon of the fatty acid chain undergoes oxidation and is converted to a carbonyl group to start the cycle all over again. Beta-oxidation is primarily facilitated by the mitochondrial trifunctional protein, an enzyme complex associated with the inner mitochondrial membrane, although very long chain fatty acids are oxidized in peroxisomes.

<span class="mw-page-title-main">Malonyl-CoA</span> Chemical compound

Malonyl-CoA is a coenzyme A derivative of malonic acid.

<span class="mw-page-title-main">Pantetheine</span> Chemical compound

Pantetheine is the cysteamine amide analog of pantothenic acid (vitamin B5). The dimer of this compound, pantethine is more commonly known, and is considered to be the most potent form of vitamin B5. Pantetheine is an intermediate in the catabolism of coenzyme A by the body.

Propionyl-CoA is a coenzyme A derivative of propionic acid. It is composed of a 24 total carbon chain and its production and metabolic fate depend on which organism it is present in. Several different pathways can lead to its production, such as through the catabolism of specific amino acids or the oxidation of odd-chain fatty acids. It later can be broken down by propionyl-CoA carboxylase or through the methylcitrate cycle. In different organisms, however, propionyl-CoA can be sequestered into controlled regions, to alleviate its potential toxicity through accumulation. Genetic deficiencies regarding the production and breakdown of propionyl-CoA also have great clinical and human significance.

<span class="mw-page-title-main">Acyl-CoA</span> Group of coenzymes that metabolize fatty acids

Acyl-CoA is a group of coenzymes that metabolize carboxylic acids. Fatty acyl-CoA's are susceptible to beta oxidation, forming, ultimately, acetyl-CoA. The acetyl-CoA enters the citric acid cycle, eventually forming several equivalents of ATP. In this way, fats are converted to ATP, the common biochemical energy carrier.

In biochemistry, fatty acid synthesis is the creation of fatty acids from acetyl-CoA and NADPH through the action of enzymes called fatty acid synthases. This process takes place in the cytoplasm of the cell. Most of the acetyl-CoA which is converted into fatty acids is derived from carbohydrates via the glycolytic pathway. The glycolytic pathway also provides the glycerol with which three fatty acids can combine to form triglycerides, the final product of the lipogenic process. When only two fatty acids combine with glycerol and the third alcohol group is phosphorylated with a group such as phosphatidylcholine, a phospholipid is formed. Phospholipids form the bulk of the lipid bilayers that make up cell membranes and surrounds the organelles within the cells. In addition to cytosolic fatty acid synthesis, there is also mitochondrial fatty acid synthesis (mtFASII), in which malonyl-CoA is formed from malonic acid with the help of malonyl-CoA synthetase (ACSF3), which then becomes the final product octanoyl-ACP (C8) via further intermediate steps.

<span class="mw-page-title-main">Long-chain-fatty-acid—CoA ligase</span> Class of enzymes

The long chain fatty acyl-CoA ligase is an enzyme of the ligase family that activates the oxidation of complex fatty acids. Long chain fatty acyl-CoA synthetase catalyzes the formation of fatty acyl-CoA by a two-step process proceeding through an adenylated intermediate. The enzyme catalyzes the following reaction,

<span class="mw-page-title-main">Carnitine palmitoyltransferase I</span> Enzyme found in humans

Carnitine palmitoyltransferase I (CPT1) also known as carnitine acyltransferase I, CPTI, CAT1, CoA:carnitine acyl transferase (CCAT), or palmitoylCoA transferase I, is a mitochondrial enzyme responsible for the formation of acyl carnitines by catalyzing the transfer of the acyl group of a long-chain fatty acyl-CoA from coenzyme A to l-carnitine. The product is often palmitoylcarnitine, but other fatty acids may also be substrates. It is part of a family of enzymes called carnitine acyltransferases. This "preparation" allows for subsequent movement of the acyl carnitine from the cytosol into the intermembrane space of mitochondria.

<span class="mw-page-title-main">Thiolase</span> Enzymes

Thiolases, also known as acetyl-coenzyme A acetyltransferases (ACAT), are enzymes which convert two units of acetyl-CoA to acetoacetyl CoA in the mevalonate pathway.

Pantothenate kinase (EC 2.7.1.33, PanK; CoaA) is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It phosphorylates pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP). It is the rate-limiting step in the biosynthesis of CoA.

<span class="mw-page-title-main">ATP citrate synthase</span> Class of enzymes

ATP citrate synthase (also ATP citrate lyase (ACLY)) is an enzyme that in animals represents an important step in fatty acid biosynthesis. By converting citrate to acetyl-CoA, the enzyme links carbohydrate metabolism, which yields citrate as an intermediate, with fatty acid biosynthesis, which consumes acetyl-CoA. In plants, ATP citrate lyase generates cytosolic acetyl-CoA precursors of thousands of specialized metabolites, including waxes, sterols, and polyketides.

<span class="mw-page-title-main">Fatty-acyl-CoA synthase</span>

Fatty-acyl-CoA synthase, or more commonly known as yeast fatty acid synthase, is an enzyme complex responsible for fatty acid biosynthesis, and is of Type I Fatty Acid Synthesis (FAS). Yeast fatty acid synthase plays a pivotal role in fatty acid synthesis. It is a 2.6 MDa barrel shaped complex and is composed of two, unique multi-functional subunits: alpha and beta. Together, the alpha and beta units are arranged in an α6β6 structure. The catalytic activities of this enzyme complex involves a coordination system of enzymatic reactions between the alpha and beta subunits. The enzyme complex therefore consists of six functional centers for fatty acid synthesis.

Fatty acyl-CoA esters are fatty acid derivatives formed of one fatty acid, a 3'-phospho-AMP linked to phosphorylated pantothenic acid (vitamin B5) and cysteamine.

References

  1. 1 2 3 4 Dawson RM, Elliott DC, Elliott WH, Jones KM (2002). Data for Biochemical Research (3rd ed.). Clarendon Press. pp. 118–119. ISBN   978-0-19-855299-4.
  2. ↑ Daugherty M, Polanuyer B, Farrell M, Scholle M, Lykidis A, de Crécy-Lagard V, Osterman A (June 2002). "Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics". The Journal of Biological Chemistry. 277 (24): 21431–21439. doi: 10.1074/jbc.M201708200 . PMID   11923312.
  3. ↑ "Coenzyme A: when small is mighty". www.asbmb.org. Archived from the original on 2018-12-20. Retrieved 2018-12-19.
  4. ↑ Lipmann F, Kaplan NO (1946). "A common factor in the enzymatic acetylation of sulfanilamide and of choline". Journal of Biological Chemistry. 162 (3): 743–744. doi: 10.1016/S0021-9258(17)41419-0 .
  5. ↑ Baddiley J, Thain EM, Novelli GD, Lipmann F (January 1953). "Structure of coenzyme A". Nature. 171 (4341): 76. Bibcode:1953Natur.171...76B. doi: 10.1038/171076a0 . PMID   13025483. S2CID   630898.
  6. 1 2 Kresge N, Simoni RD, Hill RL (2005-05-27). "Fritz Lipmann and the Discovery of Coenzyme A". Journal of Biological Chemistry. 280 (21): e18. ISSN   0021-9258. Archived from the original on 2019-04-12. Retrieved 2017-10-24.
  7. ↑ Lipmann F, Kaplan NO (March 1947). "Coenzyme for acetylation, a pantothenic acid derivative". The Journal of Biological Chemistry. 167 (3): 869–870. doi: 10.1016/S0021-9258(17)30973-0 . PMID   20287921.
  8. ↑ Lipmann F, Kaplan NO, Novelli GD, Tuttle LC, Guirard BM (September 1950). "Isolation of coenzyme A". The Journal of Biological Chemistry. 186 (1): 235–243. doi: 10.1016/S0021-9258(18)56309-2 . PMID   14778827.
  9. ↑ "Fritz Lipmann – Facts". Nobelprize.org. Nobel Media AB. 2014. Retrieved 8 November 2017.
  10. ↑ "Vitamin B5 (Pantothenic acid)". University of Maryland Medical Center. Archived from the original on 2017-10-18. Retrieved 2017-11-08.
  11. ↑ "Pantothenic Acid (Vitamin B5): MedlinePlus Supplements". medlineplus.gov. Archived from the original on 2017-12-22. Retrieved 2017-12-10.
  12. 1 2 3 4 5 Leonardi R, Jackowski S (April 2007). "Biosynthesis of Pantothenic Acid and Coenzyme A". EcoSal Plus. 2 (2). doi:10.1128/ecosalplus.3.6.3.4. PMC   4950986 . PMID   26443589.
  13. 1 2 Leonardi R, Zhang YM, Rock CO, Jackowski S (2005). "Coenzyme A: back in action". Progress in Lipid Research. 44 (2–3): 125–153. doi:10.1016/j.plipres.2005.04.001. PMID   15893380.
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  15. ↑ de Villiers M, Strauss E (October 2015). "Metabolism: Jump-starting CoA biosynthesis". Nature Chemical Biology. 11 (10): 757–758. doi:10.1038/nchembio.1912. PMID   26379022.
  16. ↑ Sibon OC, Strauss E (October 2016). "Coenzyme A: to make it or uptake it?". Nature Reviews. Molecular Cell Biology. 17 (10): 605–606. doi:10.1038/nrm.2016.110. PMID   27552973. S2CID   10344527.
  17. ↑ Mouterde LM, Stewart JD (19 December 2018). "Isolation and Synthesis of One of the Most Central Cofactors in Metabolism: Coenzyme A" (PDF). Organic Process Research & Development. 23: 19–30. doi:10.1021/acs.oprd.8b00348. S2CID   92802641.
  18. ↑ Elovson J, Vagelos PR (July 1968). "Acyl carrier protein. X. Acyl carrier protein synthetase". The Journal of Biological Chemistry. 243 (13): 3603–3611. doi: 10.1016/S0021-9258(19)34183-3 . PMID   4872726.
  19. ↑ Strickland KC, Hoeferlin LA, Oleinik NV, Krupenko NI, Krupenko SA (January 2010). "Acyl carrier protein-specific 4'-phosphopantetheinyl transferase activates 10-formyltetrahydrofolate dehydrogenase". The Journal of Biological Chemistry. 285 (3): 1627–1633. doi: 10.1074/jbc.M109.080556 . PMC   2804320 . PMID   19933275.
  20. ↑ Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002). "Chapter 2: How Cells Obtain Energy from Food". Molecular Biology of the Cell (4th ed.). Garland Science.
  21. 1 2 Shi L, Tu BP (April 2015). "Acetyl-CoA and the regulation of metabolism: mechanisms and consequences". Current Opinion in Cell Biology. 33: 125–131. doi:10.1016/j.ceb.2015.02.003. PMC   4380630 . PMID   25703630.
  22. ↑ Berg JM, Tymoczko JL, Stryer L (2002). "Acetyl Coenzyme A Carboxylase Plays a Key Role in Controlling Fatty Acid Metabolism". Biochemistry.
  23. ↑ Tsuchiya Y, Peak-Chew SY, Newell C, Miller-Aidoo S, Mangal S, Zhyvoloup A, et al. (July 2017). "Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells". The Biochemical Journal. 474 (14): 2489–2508. doi:10.1042/BCJ20170129. PMC   5509381 . PMID   28341808.
  24. 1 2 Tsuchiya Y, Zhyvoloup A, Baković J, Thomas N, Yu BY, Das S, et al. (June 2018). "Protein CoAlation and antioxidant function of coenzyme A in prokaryotic cells". The Biochemical Journal. 475 (11): 1909–1937. doi:10.1042/BCJ20180043. PMC   5989533 . PMID   29626155.
  25. ↑ Malanchuk OM, Panasyuk GG, Serbyn NM, Gout IT, Filonenko VV (2015). "Generation and characterization of monoclonal antibodies specific to Coenzyme A". Biopolymers and Cell. 31 (3): 187–192. doi: 10.7124/bc.0008DF . ISSN   0233-7657.
  26. 1 2 Tossounian MA, Baczynska M, Dalton W, Newell C, Ma Y, Das S, et al. (July 2022). "Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions". Antioxidants. 11 (7): 1362. doi: 10.3390/antiox11071362 . PMC   9312308 . PMID   35883853.
  27. ↑ Tossounian MA, Zhang B, Gout I (December 2020). "The Writers, Readers, and Erasers in Redox Regulation of GAPDH". Antioxidants. 9 (12): 1288. doi: 10.3390/antiox9121288 . PMC   7765867 . PMID   33339386.
  28. ↑ Yu BY, Tossounian MA, Hristov SD, Lawrence R, Arora P, Tsuchiya Y, et al. (August 2021). "Regulation of metastasis suppressor NME1 by a key metabolic cofactor coenzyme A". Redox Biology. 44: 101978. doi:10.1016/j.redox.2021.101978. PMC   8212152 . PMID   33903070.
  29. ↑ Baković J, Yu BY, Silva D, Chew SP, Kim S, Ahn SH, et al. (November 2019). "A key metabolic integrator, coenzyme A, modulates the activity of peroxiredoxin 5 via covalent modification". Molecular and Cellular Biochemistry. 461 (1–2): 91–102. doi:10.1007/s11010-019-03593-w. PMC   6790197 . PMID   31375973.
  30. ↑ Tossounian MA, Baczynska M, Dalton W, Peak-Chew SY, Undzenas K, Korza G, et al. (April 2023). "Bacillus subtilis YtpP and Thioredoxin A Are New Players in the Coenzyme-A-Mediated Defense Mechanism against Cellular Stress". Antioxidants. 12 (4): 938. doi: 10.3390/antiox12040938 . PMC   10136147 . PMID   37107313.
  31. ↑ "Datasheet for free acid coenzyme A" (PDF). Oriental Yeast Co., LTD.
  32. ↑ "Datasheet for lithium salt coenzyme A" (PDF). Oriental Yeast Co., LTD.

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