View source for Butyryl-CoA

{{cs1 config|name-list-style=vanc|display-authors=6}}
{{Chembox
| ImageFile = Butyryl coenzyme A.svg
| ImageFile_Ref = {{chemboximage|correct|??}}
| ImageSize = 244
| ImageName = Stereo skeletal formula of tetradeprotonated butyryl-coA ({[(2''R'',3''S'',4''R'',5''R'')-5-yl,-2-meth,-4-hydrox,-3-yl]})
| IUPACName = 3′-''O''-Phosphonoadenosine 5′-<nowiki/>{[(2''R'',3''S'',4''R'',5''R'')-5-(6-Amino-9''H''-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methyl} ''O''<sup>3</sup>-<nowiki/>{(3''R'')-4-[(3-{[2-(butanoylsulfanyl)ethyl]amino}-3-oxopropyl)amino]-3-hydroxy-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate}
| SystematicName = ''O''<sup>1</sup>-<nowiki/>{[(2''R'',3''S'',4''R'',5''R'')-5-(6-Amino-9''H''-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methyl} ''O''<sup>3</sup>-<nowiki/>{(3''R'')-4-[(3-{[2-(butanoylsulfanyl)ethyl]amino}-3-oxopropyl)amino]-3-hydroxy-2,2-dimethyl-4-oxobutyl} dihydrogen diphosphate
|Section1={{Chembox Identifiers
| CASNo = 2140-48-9
| CASNo_Ref = {{cascite|changed|??}}
| PubChem = 265
| PubChem1 = 25201345
| PubChem1_Comment = <small>{[(2''R'',5''R'')-5-yl,-2-({[{[(3''R'')-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]}</small>
| PubChem2 = 439173
| PubChem2_Comment = <small>{[(2''R'',3''S'',4''R'',5''R'')-5-yl,-2-meth,-4-hydrox,-3-yl]}</small>
| PubChem3 = 46907881
| PubChem3_Comment = <small>{[(2''R'',3''R'',5''R'')-5-yl,-2-({[{[(3''R'')-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]}</small>
| PubChem4 = 6917112
| PubChem4_Comment = <small>{[(2''R'',3''R'',5''R'')-5-yl,-2-({[{[(3''S'')-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]}</small>
| ChemSpiderID = 260
| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}
| ChemSpiderID1 = 388318
| ChemSpiderID1_Ref = {{chemspidercite|correct|chemspider}}
| ChemSpiderID1_Comment = <small>{[(2''R'',3''S'',4''R'',5''R'')-5-yl,-2-meth,-4-hydrox,-3-yl]}</small>
| ChemSpiderID2 = 5292369
| ChemSpiderID2_Ref = {{chemspidercite|correct|chemspider}}
| ChemSpiderID2_Comment = <small>{[(2''R'',3''R'',5''R'')-5-yl,-2-({[{[(3''S'')-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]}</small>
| KEGG = C00136
| KEGG_Ref = {{keggcite|correct|kegg}}
| MeSHName = butyryl-coenzyme+A
| ChEBI = 15517
| 3DMet = B04811
| SMILES = 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
| StdInChI = 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)
| StdInChI_Ref = {{stdinchicite|correct|chemspider}}
| StdInChIKey = CRFNGMNYKDXRTN-UHFFFAOYSA-N
| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}}
}}
|Section2={{Chembox Properties
| C=25 | H=42 | N=7 | O=17 | P=3 | S=1 
}}
}}
'''Butyryl-CoA''' (or '''butyryl-coenzyme A, butanoyl-CoA''') is an [[Organic compound|organic]] [[coenzyme A]]-containing derivative of [[butyric acid]].<ref>{{Cite web |title=Human Metabolome Database: Showing metabocard for Butyryl-CoA (HMDB0001088) |url=http://www.hmdb.ca/metabolites/HMDB0001088}}</ref> It is a natural product found in many biological pathways, such as [[fatty acid metabolism]] ([[Fatty acid degradation|degradation]] and [[Fatty acid synthesis|elongation]]), [[fermentation]], and 4-aminobutanoate (GABA) degradation. It mostly participates as an intermediate, a precursor to and converted from crotonyl-CoA.<ref name="ReferenceA">{{Cite journal |last1=Li |first1=Fuli |last2=Hinderberger |first2=Julia |last3=Seedorf |first3=Henning |last4=Zhang |first4=Jin |last5=Buckel |first5=Wolfgang |last6=Thauer |first6=Rudolf K. |date=February 2008 |title=Coupled Ferredoxin and Crotonyl Coenzyme A (CoA) Reduction with NADH Catalyzed by the Butyryl-CoA Dehydrogenase/Etf Complex from Clostridium kluyveri |journal=Journal of Bacteriology |language=en |volume=190 |issue=3 |pages=843–850 |doi=10.1128/JB.01417-07 |issn=0021-9193 |pmc=2223550 |pmid=17993531}}</ref> 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&nbsp;°C. Therefore, changes above from this value will denature the enzyme.<ref>{{cite journal |vauthors=Berzin V, Tyurin M, Kiriukhin M |date=February 2013 |title=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 |journal=Applied Biochemistry and Biotechnology |volume=169 |issue=3 |pages=950–959 |doi=10.1007/s12010-012-0060-7 |pmid=23292245 |s2cid=22534861}}</ref>

Within the human colon, butyrate helps supply energy to the gut epithelium and helps regulate cell responses.<ref>{{cite journal |vauthors=Louis P, Young P, Holtrop G, Flint HJ |date=February 2010 |title=Diversity of human colonic butyrate-producing bacteria revealed by analysis of the butyryl-CoA:acetate CoA-transferase gene |journal=Environmental Microbiology |volume=12 |issue=2 |pages=304–314 |doi=10.1111/j.1462-2920.2009.02066.x |pmid=19807780|bibcode=2010EnvMi..12..304L }}</ref>

Butyryl-CoA has a very high calculated potential Gibbs energy, -462.53937 kcal/mol, stored at its bond with CoA.<ref>{{Cite web |title=MetaCyc butanoyl-CoA |url=https://metacyc.org/compound?orgid=META&id=BUTYRYL-COA |access-date=2024-04-04 |website=metacyc.org}}</ref>

== Reaction ==

=== Fatty acid metabolism ===
Butyryl-CoA interconverts to and from 3-oxohexanoyl-CoA by acetyl-CoA acetyltransferase (or [[thiolase]]).<ref>{{Cite journal |last1=Fujita |first1=Yasutaro |last2=Matsuoka |first2=Hiroshi |last3=Hirooka |first3=Kazutake |date=November 2007 |title=Regulation of Fatty Acid Metabolism in Bacteria |url=https://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2007.05947.x |journal=Molecular Microbiology |language=en |volume=66 |issue=4 |pages=829–839 |doi=10.1111/j.1365-2958.2007.05947.x |pmid=17919287 |issn=0950-382X}}</ref> In terms of organic chemistry, the reaction is the reverse of a [[Claisen condensation]].<ref>{{Cite journal |last1=Haapalainen |first1=Antti M. |last2=Meriläinen |first2=Gitte |last3=Pirilä |first3=Päivi L. |last4=Kondo |first4=Naomi |last5=Fukao |first5=Toshiyuki |last6=Wierenga |first6=Rik K. |date=2007-04-10 |title=Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function |url=https://pubmed.ncbi.nlm.nih.gov/17371050/ |journal=Biochemistry |volume=46 |issue=14 |pages=4305–4321 |doi=10.1021/bi6026192 |issn=0006-2960 |pmid=17371050}}</ref><ref name=":32">{{Cite journal |last1=Haapalainen |first1=Antti M. |last2=Meriläinen |first2=Gitte |last3=Pirilä |first3=Päivi L. |last4=Kondo |first4=Naomi |last5=Fukao |first5=Toshiyuki |last6=Wierenga |first6=Rik K. |date=2007-03-20 |title=Crystallographic and Kinetic Studies of Human Mitochondrial Acetoacetyl-CoA Thiolase: The Importance of Potassium and Chloride Ions for Its Structure and Function<sup>,</sup> |url=https://pubmed.ncbi.nlm.nih.gov/17371050/ |journal=Biochemistry |language=en |volume=46 |issue=14 |pages=4305–4321 |doi=10.1021/bi6026192 |pmid=17371050 |issn=0006-2960}}</ref><ref name=":42">{{Cite journal |last1=Nesbitt |first1=Natasha M. |last2=Yang |first2=Xinxin |last3=Fontán |first3=Patricia |last4=Kolesnikova |first4=Irina |last5=Smith |first5=Issar |last6=Sampson |first6=Nicole S. |last7=Dubnau |first7=Eugenie |date=January 2010 |title=A Thiolase of Mycobacterium tuberculosis Is Required for Virulence and Production of Androstenedione and Androstadienedione from Cholesterol |journal=Infection and Immunity |language=en |volume=78 |issue=1 |pages=275–282 |doi=10.1128/IAI.00893-09 |issn=0019-9567 |pmc=2798224 |pmid=19822655}}</ref><ref>{{Cite journal |last1=Stern |first1=J. R. |last2=Coon |first2=M. J. |last3=Del Campillo |first3=A. |date=1953-01-03 |title=Enzymatic breakdown and synthesis of acetoacetate |url=https://pubmed.ncbi.nlm.nih.gov/13025466/ |journal=Nature |volume=171 |issue=4340 |pages=28–30 |doi=10.1038/171028a0 |issn=0028-0836 |pmid=13025466|bibcode=1953Natur.171...28S }}</ref><ref>{{Cite journal |last=Goldman |first=D. S. |date=May 1954 |title=Studies on the fatty acid oxidizing system of animal tissues. VII. The beta-ketoacyl coenzyme A cleavage enzyme |journal=The Journal of Biological Chemistry |volume=208 |issue=1 |pages=345–357 |doi=10.1016/S0021-9258(18)65653-4 |doi-access=free |issn=0021-9258 |pmid=13174544}}</ref> Subsequently butyryl-CoA is converted into crotonyl-CoA. The conversion is catalyzed by electron-transfer flavoprotein 2,3-oxidoreductase.<ref name="ReferenceB">{{Cite journal |last1=Campbell |first1=John W. |last2=Cronan |first2=John E. |date=July 2002 |title=The Enigmatic Escherichia coli fadE Gene Is yafH |journal=Journal of Bacteriology |language=en |volume=184 |issue=13 |pages=3759–3764 |doi=10.1128/JB.184.13.3759-3764.2002 |issn=0021-9193 |pmc=135136 |pmid=12057976}}</ref> This enzyme has many synonyms that are [[Orthology (language)|orthologous]] to each other, including butyryl-CoA dehydrogenase,<ref name="ReferenceB"/><ref>{{Cite journal |last1=Ikeda |first1=Y. |last2=Okamura-Ikeda |first2=K. |last3=Tanaka |first3=K. |date=1985-01-25 |title=Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme |journal=The Journal of Biological Chemistry |volume=260 |issue=2 |pages=1311–1325 |doi=10.1016/S0021-9258(20)71245-7 |doi-access=free |issn=0021-9258 |pmid=3968063}}</ref><ref>{{Cite journal |last1=Matsubara |first1=Y. |last2=Indo |first2=Y. |last3=Naito |first3=E. |last4=Ozasa |first4=H. |last5=Glassberg |first5=R. |last6=Vockley |first6=J. |last7=Ikeda |first7=Y. |last8=Kraus |first8=J. |last9=Tanaka |first9=K. |date=1989-09-25 |title=Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family |journal=The Journal of Biological Chemistry |volume=264 |issue=27 |pages=16321–16331 |doi=10.1016/S0021-9258(18)71624-4 |doi-access=free |issn=0021-9258 |pmid=2777793}}</ref> [[acyl-CoA dehydrogenase]],<ref>{{Cite journal |last1=Kim |first1=J J |last2=Wang |first2=M |last3=Paschke |first3=R |date=1993-08-15 |title=Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. |journal=Proceedings of the National Academy of Sciences |language=en |volume=90 |issue=16 |pages=7523–7527 |doi=10.1073/pnas.90.16.7523 |doi-access=free |issn=0027-8424 |pmc=47174 |pmid=8356049|bibcode=1993PNAS...90.7523K }}</ref> acyl-CoA oxidase,<ref>{{Cite journal |last1=VANHOOREN |first1=Johannes C. T. |last2=MARYNEN |first2=Peter |last3=MANNAERTS |first3=Guy P. |last4=VAN VELDHOVEN |first4=Paul P. |date=1997-08-01 |title=Evidence for the existence of a pristanoyl-CoA oxidase gene in man |url=https://doi.org/10.1042/bj3250593 |journal=Biochemical Journal |volume=325 |issue=3 |pages=593–599 |doi=10.1042/bj3250593 |issn=0264-6021 |pmc=1218600 |pmid=9271077}}</ref> and short-chain 2-methylacyl-CoA dehydrogenase<ref>{{Cite journal |last1=Willard |first1=Jan |last2=Vicanek |first2=Caroline |last3=Battaile |first3=Kevin P. |last4=Van Veldhoven |first4=Paul P. |last5=Fauq |first5=Abdul H. |last6=Rozen |first6=Rima |last7=Vockley |first7=Jerry |date=1996-07-01 |title=Cloning of a cDNA for Short/Branched Chain Acyl-Coenzyme A Dehydrogenase from Rat and Characterization of Its Tissue Expression and Substrate Specificity |url=https://www.sciencedirect.com/science/article/pii/S0003986196902908 |journal=Archives of Biochemistry and Biophysics |volume=331 |issue=1 |pages=127–133 |doi=10.1006/abbi.1996.0290 |pmid=8660691 |issn=0003-9861|url-access=subscription }}</ref>

=== Fermentation ===
'''Butyryl-CoA''' is an intermediate of the fermentation pathway found in ''[[Clostridium kluyveri]]''.<ref>{{Cite journal |last1=Barker |first1=H. A. |last2=Kamen |first2=M. D. |last3=Bornstein |first3=B. T. |date=December 1945 |title=The Synthesis of Butyric and Caproic Acids from Ethanol and Acetic Acid by Clostridium Kluyveri |journal=Proceedings of the National Academy of Sciences |language=en |volume=31 |issue=12 |pages=373–381 |doi=10.1073/pnas.31.12.373 |doi-access=free |issn=0027-8424 |pmc=1078850 |pmid=16588706|bibcode=1945PNAS...31..373B }}</ref><ref name=":12">{{Cite journal |last1=Bornstein |first1=B. T. |last2=Barker |first2=H. A. |date=February 1948 |title=The energy metabolism of Clostridium kluyveri and the synthesis of fatty acids |journal=The Journal of Biological Chemistry |volume=172 |issue=2 |pages=659–669 |doi=10.1016/S0021-9258(19)52752-1 |doi-access=free |issn=0021-9258 |pmid=18901185}}</ref><ref name=":22">{{Cite journal |last1=Kenealy |first1=William R. |last2=Waselefsky |first2=David M. |date=April 1985 |title=Studies on the substrate range of Clostridium kluyveri; the use of propanol and succinate |url=http://link.springer.com/10.1007/BF00408056 |journal=Archives of Microbiology |language=en |volume=141 |issue=3 |pages=187–194 |doi=10.1007/BF00408056 |bibcode=1985ArMic.141..187K |issn=0302-8933|url-access=subscription }}</ref> This species can ferment acetyl-CoA and [[succinate]] into [[butanoate]], extracting energy through the process.<ref name=":12" /><ref name=":22" /> The fermentation pathway from ethanol to acetyl-CoA to butanoate is also known as [[Acetone–butanol–ethanol fermentation|ABE fermentation]]. 
[[File:Overview_of_fermentation_pathways_with_butyryl-CoA.png|left|thumb|236x236px|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]]<nowiki/>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.<ref name="ReferenceA"/><ref>{{Cite journal |last1=Williamson |first1=G |last2=Engel |first2=P C |date=1984-03-01 |title=Butyryl-CoA dehydrogenase from Megasphaera elsdenii . Specificity of the catalytic reaction |url=https://portlandpress.com/biochemj/article/218/2/521/17032/Butyryl-CoA-dehydrogenase-from-Megasphaera |journal=Biochemical Journal |language=en |volume=218 |issue=2 |pages=521–529 |doi=10.1042/bj2180521 |issn=0264-6021 |pmc=1153368 |pmid=6712628}}</ref><ref>{{Cite journal |last1=Turano |first1=F. J. |last2=Thakkar |first2=S. S. |last3=Fang |first3=T. |last4=Weisemann |first4=J. M. |date=1997-04-01 |title=Characterization and Expression of NAD(H)-Dependent Glutamate Dehydrogenase Genes in Arabidopsis |journal=Plant Physiology |language=en |volume=113 |issue=4 |pages=1329–1341 |doi=10.1104/pp.113.4.1329 |issn=1532-2548 |pmc=158256 |pmid=9112779}}</ref> Subsequently, butyryl-CoA is converted into butanoate by propionyl-CoA transferase, which transfers the coenzyme-A group onto an [[acetate]], forming [[acetyl-CoA]].<ref>{{Cite journal |last1=Rangarajan |first1=Erumbi S. |last2=Li |first2=Yunge |last3=Ajamian |first3=Eunice |last4=Iannuzzi |first4=Pietro |last5=Kernaghan |first5=Stephanie D. |last6=Fraser |first6=Marie E. |last7=Cygler |first7=Miroslaw |last8=Matte |first8=Allan |date=December 2005 |title=Crystallographic Trapping of the Glutamyl-CoA Thioester Intermediate of Family I CoA Transferases |journal=Journal of Biological Chemistry |language=en |volume=280 |issue=52 |pages=42919–42928 |doi=10.1074/jbc.M510522200|doi-access=free |pmid=16253988 }}</ref><ref>{{Cite journal |last1=Vanderwinkel |first1=Edgard |last2=Furmanski |first2=Philip |last3=Reeves |first3=Henry C. |last4=Ajl |first4=Samuel J. |date=December 1968 |title=Growth of Escherichiacoli on fatty acids: Requirement for coenzyme a transferase activity |url=https://linkinghub.elsevier.com/retrieve/pii/0006291X68903975 |journal=Biochemical and Biophysical Research Communications |language=en |volume=33 |issue=6 |pages=902–908 |doi=10.1016/0006-291X(68)90397-5|pmid=4884054 |url-access=subscription }}</ref>
[[File:Conversion_from_crotonyl-CoA_to_butanoyl-CoA_to_butanoate.png|center|thumb|316x316px|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.<ref>{{cite journal |vauthors=Demmer JK, Pal Chowdhury N, Selmer T, Ermler U, Buckel W |date=November 2017 |title=The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile |journal=Nature Communications |volume=8 |issue=1 |pages=1577 |bibcode=2017NatCo...8.1577D |doi=10.1038/s41467-017-01746-3 |pmc=5691135 |pmid=29146947}}</ref>

=== 4-aminobutanoate (GABA) degradation ===
[[File:Overview_of_GABA_Degradation.png|thumb|260x260px|Overview of '''4-aminobutanoate (GABA) degradation''']]
'''Butyryl-CoA''' is also an intermediate found in [[4-aminobutanoate]] (GABA) degradation.<ref name=":02">{{Cite journal |last1=Belitsky |first1=Boris R. |last2=Sonenshein |first2=Abraham L. |date=July 2002 |title=GabR, a member of a novel protein family, regulates the utilization of γ -aminobutyrate in Bacillus subtilis |url=https://onlinelibrary.wiley.com/doi/10.1046/j.1365-2958.2002.03036.x |journal=Molecular Microbiology |language=en |volume=45 |issue=2 |pages=569–583 |doi=10.1046/j.1365-2958.2002.03036.x |pmid=12123465 |issn=0950-382X}}</ref> [[Γ-Aminobutyric acid|4-aminobutanoate]] (GABA) has two fates in this degradation pathway. When discovered in ''[[Acetoanaerobium sticklandii]]'' and ''[[Pseudomonas fluorescens]]'', 4-aminobutanoate was converted into ''[[L-glutamate|glutamate]]'', which can be deaminated, releasing [[ammonium]].<ref>{{Cite journal |last1=Hardman |first1=John K. |last2=Stadtman |first2=Thressa C. |date=April 1960 |title=METABOLISM OF ω-AMINO ACIDS: I. Fermentation of γ-Aminobutyric Acid by Clostridium aminobutyricum n. sp. |journal=Journal of Bacteriology |language=en |volume=79 |issue=4 |pages=544–548 |doi=10.1128/jb.79.4.544-548.1960 |issn=0021-9193 |pmc=278728 |pmid=14399736}}</ref><ref>{{Cite journal |last1=Hardman |first1=J. K. |last2=Stadtman |first2=T. C. |date=June 1963 |title=Metabolism of amega-amino acids. III. Mechanism of conversion of gamma-aminobutyrate to gamma-hydroxybutryate by Clostridium aminobutyricum |journal=The Journal of Biological Chemistry |volume=238 |issue=6 |pages=2081–2087 |doi=10.1016/S0021-9258(18)67943-8 |doi-access=free |issn=0021-9258 |pmid=13952769}}</ref><ref>{{Cite journal |last1=Andersen |first1=Gorm |last2=Andersen |first2=Birgit |last3=Dobritzsch |first3=Doreen |last4=Schnackerz |first4=Klaus D. |last5=Piškur |first5=Jure |date=April 2007 |title=A gene duplication led to specialized γ-aminobutyrate and β-alanine aminotransferase in yeast |url=https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2007.05729.x |journal=The FEBS Journal |language=en |volume=274 |issue=7 |pages=1804–1817 |doi=10.1111/j.1742-4658.2007.05729.x |pmid=17355287 |issn=1742-464X}}</ref> 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]].<ref>{{Cite journal |last1=Gerhardt |first1=Astrid |last2=Çinkaya |first2=Irfan |last3=Linder |first3=Dietmar |last4=Huisman |first4=Gjalt |last5=Buckel |first5=Wolfgang |date=2000-08-30 |title=Fermentation of 4-aminobutyrate by Clostridium aminobutyricum : cloning of two genes involved in the formation and dehydration of 4-hydroxybutyryl-CoA |url=http://link.springer.com/10.1007/s002030000195 |journal=Archives of Microbiology |volume=174 |issue=3 |pages=189–199 |doi=10.1007/s002030000195 |pmid=11041350 |bibcode=2000ArMic.174..189G |issn=0302-8933|url-access=subscription }}</ref><ref>{{Cite journal |last1=Jakoby |first1=W. B. |last2=Scott |first2=E. M. |date=April 1959 |title=Aldehyde oxidation. III. Succinic semialdehyde dehydrogenase |journal=The Journal of Biological Chemistry |volume=234 |issue=4 |pages=937–940 |doi=10.1016/S0021-9258(18)70207-X |doi-access=free |issn=0021-9258 |pmid=13654295}}</ref>

The degradation pathway plays an important role in regulating the concentration of GABA, which is an inhibitory [[neurotransmitter]] that reduces neuronal excitability.<ref>{{Cite journal |last1=Li |first1=Ke |last2=Xu |first2=En |date=2008-06-01 |title=The role and the mechanism of γ-aminobutyric acid during central nervous system development |url=https://doi.org/10.1007/s12264-008-0109-3 |journal=Neuroscience Bulletin |language=en |volume=24 |issue=3 |pages=195–200 |doi=10.1007/s12264-008-0109-3 |issn=1995-8218 |pmc=5552538 |pmid=18500393}}</ref> Dysregulation of GABA degradation can lead to imbalances in neurotransmitter levels, contributing to various [[neurological disorder]]s such as [[epilepsy]], [[anxiety]], and [[Depression (mood)|depression]].<ref>{{Citation |last1=de Leon |first1=Anthony S. |title=Biochemistry, Gamma Aminobutyric Acid |date=2024 |work=StatPearls |url=http://www.ncbi.nlm.nih.gov/books/NBK551683/ |access-date=2024-04-14 |place=Treasure Island (FL) |publisher=StatPearls Publishing |pmid=31869147 |last2=Tadi |first2=Prasanna}}</ref><ref>{{Cite journal |last1=Donahue |first1=Manus J. |last2=Near |first2=Jamie |last3=Blicher |first3=Jakob U. |last4=Jezzard |first4=Peter |date=2010-11-01 |title=Baseline GABA concentration and fMRI response |url=https://www.sciencedirect.com/science/article/pii/S1053811910009687 |journal=NeuroImage |volume=53 |issue=2 |pages=392–398 |doi=10.1016/j.neuroimage.2010.07.017 |pmid=20633664 |issn=1053-8119|url-access=subscription }}</ref> 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.<ref name=":02" />

== Regulation ==
Butyryl-CoA acts upon [[Butanal dehydrogenase|butanol dehydrogenase]] via [[competitive inhibition]]. The adenine moiety can bind butanol dehydrogenase and reduce its activity.<ref>{{Cite journal |last1=Welch |first1=Richard W. |last2=Rudolph |first2=Frederick B. |last3=Papoutsakis |first3=E.Terry |date=September 1989 |title=Purification and characterization of the NADH-dependent butanol dehydrogenase from Clostridium acetobutylicum (ATCC 824) |url=https://linkinghub.elsevier.com/retrieve/pii/000398618990489X |journal=Archives of Biochemistry and Biophysics |language=en |volume=273 |issue=2 |pages=309–318 |doi=10.1016/0003-9861(89)90489-X|pmid=2673038 |url-access=subscription }}</ref> The phosphate moiety of butyryl-CoA is found to have inhibitory activities upon its binding with phosphotransbutyrylase.<ref>{{Cite journal |last1=Wiesenborn |first1=D P |last2=Rudolph |first2=F B |last3=Papoutsakis |first3=E T |date=February 1989 |title=Phosphotransbutyrylase from Clostridium acetobutylicum ATCC 824 and its role in acidogenesis |journal=Applied and Environmental Microbiology |language=en |volume=55 |issue=2 |pages=317–322 |doi=10.1128/aem.55.2.317-322.1989 |issn=0099-2240 |pmc=184108 |pmid=2719475|bibcode=1989ApEnM..55..317W }}</ref>

Butyryl-CoA is also believed to have inhibitory effects on [[Acetyl-CoA-acetyl transferase|acetyl-CoA acetyltransferase]],<ref>{{Cite journal |last1=Wiesenborn |first1=Dennis P. |last2=Rudolph |first2=Frederick B. |last3=Papoutsakis |first3=Eleftherios T. |date=November 1988 |title=Thiolase from Clostridium acetobutylicum ATCC 824 and Its Role in the Synthesis of Acids and Solvents |journal=Applied and Environmental Microbiology |language=en |volume=54 |issue=11 |pages=2717–2722 |doi=10.1128/aem.54.11.2717-2722.1988 |issn=0099-2240 |pmc=204361 |pmid=16347774|bibcode=1988ApEnM..54.2717W }}</ref> DL-methylmalonyl-CoA racemase,<ref>{{Cite journal |last1=Stabler |first1=Sally P. |last2=Marcell |first2=Paul D. |last3=Allen |first3=Robert H. |date=August 1985 |title=Isolation and characterization of dl-methylmalonyl-coenzyme A racemase from rat liver |url=https://linkinghub.elsevier.com/retrieve/pii/0003986185903819 |journal=Archives of Biochemistry and Biophysics |language=en |volume=241 |issue=1 |pages=252–264 |doi=10.1016/0003-9861(85)90381-9|pmid=2862845 |url-access=subscription }}</ref> and [[glycine N-acyltransferase]],<ref>{{Cite journal |last1=Nandi |first1=D. L. |last2=Lucas |first2=S. V. |last3=Webster |first3=L. T. |date=1979-08-10 |title=Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization |journal=The Journal of Biological Chemistry |volume=254 |issue=15 |pages=7230–7237 |doi=10.1016/S0021-9258(18)50309-4 |doi-access=free |issn=0021-9258 |pmid=457678}}</ref> however, the specific mechanism remains unknown.

==Further reading==
{{Cite web|last=PubChem|title=Butyryl-CoA|url=https://pubchem.ncbi.nlm.nih.gov/compound/122283|access-date=2021-11-18|website=pubchem.ncbi.nlm.nih.gov|language=en}}

== See also ==
* [[Acyl-CoA]]
** [[Fatty acyl-CoA esters]]

== References ==
{{reflist}}

[[Category:Thioesters of coenzyme A]]