Butyryl-CoA

Last updated
Butyryl-CoA
Butyryl coenzyme A.svg
Names
IUPAC name
3′-O-Phosphonoadenosine 5′-{[(2R,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methyl} O3-{(3R)-4-[(3-{[2-(butanoylsulfanyl)ethyl]amino}-3-oxopropyl)amino]-3-hydroxy-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate}
Systematic IUPAC name
O1-{[(2R,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methyl} O3-{(3R)-4-[(3-{[2-(butanoylsulfanyl)ethyl]amino}-3-oxopropyl)amino]-3-hydroxy-2,2-dimethyl-4-oxobutyl} dihydrogen diphosphate
Identifiers
3D model (JSmol)
3DMet
ChEBI
ChemSpider
  • 260  Yes check.svgY
  • 388318 {[(2R,3S,4R,5R)-5-yl,-2-meth,-4-hydrox,-3-yl]} Yes check.svgY
  • 5292369 {[(2R,3R,5R)-5-yl,-2-({[{[(3S)-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]} Yes check.svgY
KEGG
MeSH butyryl-coenzyme+A
PubChem CID
  • 265
  • 25201345  {[(2R,5R)-5-yl,-2-({[{[(3R)-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]}
  • 439173  {[(2R,3S,4R,5R)-5-yl,-2-meth,-4-hydrox,-3-yl]}
  • 46907881  {[(2R,3R,5R)-5-yl,-2-({[{[(3R)-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]}
  • 6917112  {[(2R,3R,5R)-5-yl,-2-({[{[(3S)-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]}
  • InChI=1S/C25H42N7O17P3S/c1-4-5-16(34)53-9-8-27-15(33)6-7-28-23(37)20(36)25(2,3)11-46-52(43,44)49-51(41,42)45-10-14-19(48-50(38,39)40)18(35)24(47-14)32-13-31-17-21(26)29-12-30-22(17)32/h12-14,18-20,24,35-36H,4-11H2,1-3H3,(H,27,33)(H,28,37)(H,41,42)(H,43,44)(H2,26,29,30)(H2,38,39,40) Yes check.svgY
    Key: CRFNGMNYKDXRTN-UHFFFAOYSA-N Yes check.svgY
  • CCCC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12
Properties
C25H42N7O17P3S
Molar mass 837.62 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).

Butyryl-CoA (or butyryl-coenzyme A, butanoyl-CoA) is an organic coenzyme A-containing derivative of butyric acid. [1] It is a natural product found in many biological pathways, such as fatty acid metabolism (degradation and elongation), fermentation, and 4-aminobutanoate (GABA) degradation. It mostly participates as an intermediate, a precursor to and converted from crotonyl-CoA. [2] This interconversion is mediated by butyryl-CoA dehydrogenase.

Contents

From redox data, butyryl-CoA dehydrogenase shows little to no activity at pH higher than 7.0. This is important as enzyme midpoint potential is at pH 7.0 and at 25 °C. Therefore, changes above from this value will denature the enzyme. [3]

Within the human colon, butyrate helps supply energy to the gut epithelium and helps regulate cell responses. [4]

Butyryl-CoA has a very high potential Gibbs energy, -462.53937 kcal/mol, stored at its bond with CoA. [5]

Reaction

Fatty acid metabolism

Butyryl-CoA interconverts to and from 3-oxohexanoyl-CoA by acetyl-CoA acetyltransferase (or thiolase). [6] In terms of organic chemistry, the reaction is the reverse of a Claisen condensation. [7] [8] [9] [10] [11] [12] Subsequently butyryl-CoA is converted into crotonyl-CoA. The conversion is catalyzed by electron-transfer flavoprotein 2,3-oxidoreductase. [13] This enzyme has many synonyms that are orthologous to each other, including butyryl-CoA dehydrogenase [14] [15] [16] , acyl-CoA dehydrogenase [17] , acyl-CoA oxidase [18] , and short-chain 2-methylacyl-CoA dehydrogenase [19]

Fermentation

Butyryl-CoA is an intermediate of the fermentation pathway found in Clostridium kluyveri. [20] [21] [22] This species can ferment acetyl-CoA and succinate into butanoate, extracting energy through the process. [21] [22] The fermentation pathway from ethanol to acetyl-CoA to butanoate is also known as ABE fermentation.

Overview of fermentation pathways in Clostridium kluyveri. The red arrow is the succinate fermentation pathway; the blue arrow is the ethanol/acetyl-CoA fermentation pathway, also known as ABE fermentation. Overview of fermentation pathways with butyryl-CoA.png
Overview of fermentation pathways in Clostridium kluyveri. The red arrow is the succinate fermentation pathway; the blue arrow is the ethanol/acetyl-CoA fermentation pathway, also known as ABE fermentation.

Butyryl-CoA is reduced from crotonyl-CoA catalyzing by butyryl-CoA dehydrogenase, where two NADH molecules donate four electrons, with two of them reducing ferredoxin ([2Fe-2S] cluster) and the other two reducing crotonyl-CoA into butyryl-CoA. [23] [24] [25] Subsequently, butyryl-CoA is converted into butanoate by propionyl-CoA transferase, which transfers the coenzyme-A group onto an acetate, forming acetyl-CoA. [26] [27]

Conversion from crotonyl-CoA to butyryl-CoA to butanoate Conversion from crotonyl-CoA to butanoyl-CoA to butanoate.png
Conversion from crotonyl-CoA to butyryl-CoA to butanoate

It is essential in reducing ferredoxins in anaerobic bacteria and archaea so that electron transport phosphorylation and substrate-level phosphorylation can occur with increased efficiency. [28]

4-aminobutanoate (GABA) degradation

Overview of 4-aminobutanoate (GABA) degradation Overview of GABA Degradation.png
Overview of 4-aminobutanoate (GABA) degradation

Butyryl-CoA is also an intermediate found in 4-aminobutanoate (GABA) degradation. [29] 4-aminobutanoate (GABA) has two fates in this degradation pathway. When discovered in Acetoanaerobium sticklandii and Pseudomonas fluorescens , 4-aminobutanoate was converted into glutamate , which can be deaminated, releasing ammonium. [30] [31] [32] However, in Acetoanaerobium sticklandii and Clostridium aminobutyricum, 4-aminobutanoate was converted into succinate semialdehyde and, through a series of steps via the intermediate of butanoyl-CoA, finally converted into butanoate. [33] [34]

The degradation pathway plays an important role in regulating the concentration of GABA, which is an inhibitory neurotransmitter that reduces neuronal excitability. [35] Dysregulation of GABA degradation can lead to imbalances in neurotransmitter levels, contributing to various neurological disorders such as epilepsy, anxiety, and depression. [36] [37] The reaction mechanism is the same as that in the fermentation pathway, where butyryl-CoA is first reduced from crotonyl-CoA and then converted into butanoate. [29]

Regulation

Butyryl-CoA acts upon butanol dehydrogenase via competitive inhibition. The adenine moiety can bind butanol dehydrogenase and reduce its activity. [38] The phosphate moiety of butyryl-CoA is found to have inhibitory activities upon its binding with phosphotransbutyrylase. [39]

Butyryl-CoA is also believed to have inhibitory effects on acetyl-CoA acetyltransferase [40] , DL-methylmalonyl-CoA racemase [41] , and glycine N-acyltransferase [42] , however, the specific mechanism remains unknown.

Further reading

PubChem. "Butyryl-CoA". pubchem.ncbi.nlm.nih.gov. Retrieved 2021-11-18.

See also

Related Research Articles

<span class="mw-page-title-main">Coenzyme A</span> Coenzyme, notable for its synthesis and oxidation role

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).

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

Butyric acid, also known under the systematic name butanoic acid, is a straight-chain alkyl carboxylic acid with the chemical formula CH3CH2CH2CO2H. It is an oily, colorless liquid with an unpleasant odor. Isobutyric acid is an isomer. Salts and esters of butyric acid are known as butyrates or butanoates. The acid does not occur widely in nature, but its esters are widespread. It is a common industrial chemical and an important component in the mammalian gut.

Acyl-CoA dehydrogenases (ACADs) are a class of enzymes that function to catalyze the initial step in each cycle of fatty acid β-oxidation in the mitochondria of cells. Their action results in the introduction of a trans double-bond between C2 (α) and C3 (β) of the acyl-CoA thioester substrate. Flavin adenine dinucleotide (FAD) is a required co-factor in addition to the presence of an active site glutamate in order for the enzyme to function.

<span class="mw-page-title-main">Butanol fuel</span> Fuel for internal combustion engines

Butanol may be used as a fuel in an internal combustion engine. It is more similar to gasoline than it is to ethanol. A C4-hydrocarbon, butanol is a drop-in fuel and thus works in vehicles designed for use with gasoline without modification. Both n-butanol and isobutanol have been studied as possible fuels. Both can be produced from biomass (as "biobutanol" ) as well as from fossil fuels (as "petrobutanol"). The chemical properties depend on the isomer (n-butanol or isobutanol), not on the production method.

<span class="mw-page-title-main">Mitochondrial trifunctional protein</span> Inner mitochondrial membrane protein

Mitochondrial trifunctional protein (MTP) is a protein attached to the inner mitochondrial membrane which catalyzes three out of the four steps in beta oxidation. MTP is a hetero-octamer composed of four alpha and four beta subunits:

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">Crotonyl-CoA</span> Chemical compound

Crotonyl-coenzyme A is an intermediate in the fermentation of butyric acid, and in the metabolism of lysine and tryptophan. It is important in the metabolism of fatty acids and amino acids.

β-Hydroxybutyryl-CoA Chemical compound

β-Hydroxybutyryl-CoA is an intermediate in the fermentation of butyric acid, and in the metabolism of lysine and tryptophan. The L-3-hydroxybutyl-CoA enantiomer is also the second to last intermediate in beta oxidation of even-numbered, straight chain, and saturated fatty acids.

<span class="mw-page-title-main">3-hydroxyacyl-CoA dehydrogenase</span> Enzyme

In enzymology, a 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) is an enzyme that catalyzes the chemical reaction

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

In enzymology, a pyruvate synthase is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It is also called pyruvate:ferredoxin oxidoreductase (PFOR).

<span class="mw-page-title-main">3-oxoacid CoA-transferase</span> Enzyme family

In enzymology, a 3-oxoacid CoA-transferase is an enzyme that catalyzes the chemical reaction

In enzymology, an acetate CoA-transferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Acetyl-CoA C-acetyltransferase</span> Class of enzymes

In enzymology, an acetyl-CoA C-acetyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">4-aminobutyrate transaminase</span> Class of enzymes

In enzymology, 4-aminobutyrate transaminase, also called GABA transaminase or 4-aminobutyrate aminotransferase, or GABA-T, is an enzyme that catalyzes the chemical reaction:

<span class="mw-page-title-main">Butyrate kinase</span> Class of enzymes

In enzymology, a butyrate kinase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Short-chain acyl-CoA dehydrogenase</span>

Short-chain acyl-CoA dehydrogenase is an enzyme with systematic name short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Medium-chain acyl-CoA dehydrogenase</span>

Medium-chain acyl-CoA dehydrogenase is an enzyme with systematic name medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction

Long-chain acyl-CoA dehydrogenase is an enzyme with systematic name long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Very-long-chain acyl-CoA dehydrogenase</span>

Very-long-chain acyl-CoA dehydrogenase is an enzyme with systematic name very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction

Vincent Massey was an Australian biochemist and enzymologist best known for his contributions to the study of flavoenzymes. Massey was elected to the National Academy of Sciences in 1995 for his use of physical biochemistry to relate flavin chemistry to flavin enzymology.

References

  1. ↑ "Human Metabolome Database: Showing metabocard for Butyryl-CoA (HMDB0001088)".
  2. ↑ Li F, Hinderberger J, Seedorf H, Zhang J, Buckel W, Thauer RK (February 2008). "Coupled Ferredoxin and Crotonyl Coenzyme A (CoA) Reduction with NADH Catalyzed by the Butyryl-CoA Dehydrogenase/Etf Complex from Clostridium kluyveri". Journal of Bacteriology. 190 (3): 843–850. doi:10.1128/JB.01417-07. ISSN   0021-9193. PMC   2223550 . PMID   17993531.
  3. ↑ Berzin V, Tyurin M, Kiriukhin M (February 2013). "Selective n-butanol production by Clostridium sp. MTButOH1365 during continuous synthesis gas fermentation due to expression of synthetic thiolase, 3-hydroxy butyryl-CoA dehydrogenase, crotonase, butyryl-CoA dehydrogenase, butyraldehyde dehydrogenase, and NAD-dependent butanol dehydrogenase". Applied Biochemistry and Biotechnology. 169 (3): 950–959. doi:10.1007/s12010-012-0060-7. PMID   23292245. S2CID   22534861.
  4. ↑ Louis P, Young P, Holtrop G, Flint HJ (February 2010). "Diversity of human colonic butyrate-producing bacteria revealed by analysis of the butyryl-CoA:acetate CoA-transferase gene". Environmental Microbiology. 12 (2): 304–314. Bibcode:2010EnvMi..12..304L. doi:10.1111/j.1462-2920.2009.02066.x. PMID   19807780.
  5. ↑ "MetaCyc butanoyl-CoA". metacyc.org. Retrieved 2024-04-04.
  6. ↑ Fujita Y, Matsuoka H, Hirooka K (November 2007). "Regulation of Fatty Acid Metabolism in Bacteria". Molecular Microbiology. 66 (4): 829–839. doi:10.1111/j.1365-2958.2007.05947.x. ISSN   0950-382X. PMID   17919287.
  7. ↑ Nesbitt NM, Yang X, Fontán P, Kolesnikova I, Smith I, Sampson NS, et al. (January 2010). "A Thiolase of Mycobacterium tuberculosis Is Required for Virulence and Production of Androstenedione and Androstadienedione from Cholesterol". Infection and Immunity. 78 (1): 275–282. doi:10.1128/IAI.00893-09. ISSN   0019-9567. PMC   2798224 . PMID   19822655.
  8. ↑ Haapalainen AM, Meriläinen G, Pirilä PL, Kondo N, Fukao T, Wierenga RK (2007-04-10). "Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function". Biochemistry. 46 (14): 4305–4321. doi:10.1021/bi6026192. ISSN   0006-2960. PMID   17371050.
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  23. ↑ Li F, Hinderberger J, Seedorf H, Zhang J, Buckel W, Thauer RK (February 2008). "Coupled Ferredoxin and Crotonyl Coenzyme A (CoA) Reduction with NADH Catalyzed by the Butyryl-CoA Dehydrogenase/Etf Complex from Clostridium kluyveri". Journal of Bacteriology. 190 (3): 843–850. doi:10.1128/JB.01417-07. ISSN   0021-9193. PMC   2223550 . PMID   17993531.
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  29. 1 2 Belitsky BR, Sonenshein AL (July 2002). "GabR, a member of a novel protein family, regulates the utilization of γ -aminobutyrate in Bacillus subtilis". Molecular Microbiology. 45 (2): 569–583. doi:10.1046/j.1365-2958.2002.03036.x. ISSN   0950-382X. PMID   12123465.
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  33. ↑ Gerhardt A, Çinkaya I, Linder D, Huisman G, Buckel W (2000-08-30). "Fermentation of 4-aminobutyrate by Clostridium aminobutyricum : cloning of two genes involved in the formation and dehydration of 4-hydroxybutyryl-CoA". Archives of Microbiology. 174 (3): 189–199. Bibcode:2000ArMic.174..189G. doi:10.1007/s002030000195. ISSN   0302-8933. PMID   11041350.
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  38. ↑ Welch RW, Rudolph FB, Papoutsakis E (September 1989). "Purification and characterization of the NADH-dependent butanol dehydrogenase from Clostridium acetobutylicum (ATCC 824)". Archives of Biochemistry and Biophysics. 273 (2): 309–318. doi:10.1016/0003-9861(89)90489-X. PMID   2673038.
  39. ↑ Wiesenborn DP, Rudolph FB, Papoutsakis ET (February 1989). "Phosphotransbutyrylase from Clostridium acetobutylicum ATCC 824 and its role in acidogenesis". Applied and Environmental Microbiology. 55 (2): 317–322. Bibcode:1989ApEnM..55..317W. doi:10.1128/aem.55.2.317-322.1989. ISSN   0099-2240. PMC   184108 . PMID   2719475.
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