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Lead

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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.

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

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Fatty acid metabolism

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Butyryl-CoA is an intermediate in fatty acid metabolism, including fatty acid degradation and fatty acid elongation (or synthesis).

Fatty acid degradation

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Conversion between 3-oxohexanoyl-CoA, butyryl-CoA, and crotonyl-CoA

Butyryl-CoA is usually found at the end of fatty acid degradation, which is a key pathway a cell uses to break down fatty acids into acetyl-CoA, affording energy through the process.[6] An example of fatty acid degradation is beta-oxidation, which breaks down saturated fatty acids.

In both eukaryotes and prokaryotes, butyryl-CoA is firstly converted from 3-oxohexanoyl-CoA by acetyl-CoA acetyltransferase (or thiolase) through a reverse Claisen condensation.[7][8][9][10] This process cleaves acetyl-CoA from 3-oxohexanoyl-CoA, resulting in a product that is two carbons shorter.[11][12] The second step involves the conversion of butyryl-CoA into crotonyl-CoA. This is catalyzed by a specific enzyme called 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].

Fatty acid elongation

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The reaction mechanism is the same as that in the fatty acid degradation pathway except the direction of reaction is reversed. Thiolase catalyzes the condensation between butyryl-CoA and acetyl-CoA, forming 3-oxohexanoyl-CoA.[9][10]

Fermentation

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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.
Conversion from crotonyl-CoA to butyryl-CoA to butanoate. Cys in the ferredoxin represents the cysteine residue in the active site.

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.

Butyryl-CoA is reduced from crotonyl-CoAcatalyzing 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]

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

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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

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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.

References

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  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.
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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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  27. ^ Vanderwinkel E, Furmanski P, Reeves HC, Ajl SJ (December 1968). "Growth of Escherichiacoli on fatty acids: Requirement for coenzyme a transferase activity". Biochemical and Biophysical Research Communications. 33 (6): 902–908. doi:10.1016/0006-291X(68)90397-5. PMID 4884054.
  28. ^ Demmer JK, Pal Chowdhury N, Selmer T, Ermler U, Buckel W (November 2017). "The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile". Nature Communications. 8 (1): 1577. Bibcode:2017NatCo...8.1577D. doi:10.1038/s41467-017-01746-3. PMC 5691135. PMID 29146947.
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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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  42. ^ Nandi DL, Lucas SV, Webster LT (1979-08-10). "Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization". The Journal of Biological Chemistry. 254 (15): 7230–7237. doi:10.1016/S0021-9258(18)50309-4. ISSN 0021-9258. PMID 457678.
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