Butyryl-CoA

Last updated

Contents

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.

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 calculated 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] Subsequently butyryl-CoA is converted into crotonyl-CoA. The conversion is catalyzed by electron-transfer flavoprotein 2,3-oxidoreductase. [12] This enzyme has many synonyms that are orthologous to each other, including butyryl-CoA dehydrogenase, [12] [13] [14] acyl-CoA dehydrogenase, [15] acyl-CoA oxidase, [16] and short-chain 2-methylacyl-CoA dehydrogenase [17]

Fermentation

Butyryl-CoA is an intermediate of the fermentation pathway found in Clostridium kluyveri . [18] [19] [20] This species can ferment acetyl-CoA and succinate into butanoate, extracting energy through the process. [19] [20] 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. [2] [21] [22] Subsequently, butyryl-CoA is converted into butanoate by propionyl-CoA transferase, which transfers the coenzyme-A group onto an acetate, forming acetyl-CoA. [23] [24]

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. [25]

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. [26] 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. [27] [28] [29] 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. [30] [31]

The degradation pathway plays an important role in regulating the concentration of GABA, which is an inhibitory neurotransmitter that reduces neuronal excitability. [32] Dysregulation of GABA degradation can lead to imbalances in neurotransmitter levels, contributing to various neurological disorders such as epilepsy, anxiety, and depression. [33] [34] 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. [26]

Regulation

Butyryl-CoA acts upon butanol dehydrogenase via competitive inhibition. The adenine moiety can bind butanol dehydrogenase and reduce its activity. [35] The phosphate moiety of butyryl-CoA is found to have inhibitory activities upon its binding with phosphotransbutyrylase. [36]

Butyryl-CoA is also believed to have inhibitory effects on acetyl-CoA acetyltransferase, [37] DL-methylmalonyl-CoA racemase, [38] and glycine N-acyltransferase, [39] 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, and 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.

<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:

<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">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

Butyrate—CoA ligase, also known as xenobiotic/medium-chain fatty acid-ligase (XM-ligase), 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">Earl Reece Stadtman</span> American biochemist

Earl Reece Stadtman NAS was an American biochemist, notable for his research on enzymes and anaerobic bacteria.

Crotonyl-CoA reductase (EC 1.3.1.86, butyryl-CoA dehydrogenase, butyryl dehydrogenase, unsaturated acyl-CoA reductase, ethylene reductase, enoyl-coenzyme A reductase, unsaturated acyl coenzyme A reductase, butyryl coenzyme A dehydrogenase, short-chain acyl CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl CoA reductase, butanoyl-CoA:(acceptor) 2,3-oxidoreductase, CCR) is an enzyme with systematic name butanoyl-CoA:NADP+ 2,3-oxidoreductase. This enzyme catalyses the following 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.

<span class="mw-page-title-main">ABAT</span> Protein-coding gene in the species Homo sapiens

4-Aminobutyrate aminotransferase is a protein that in humans is encoded by the ABAT gene. This gene is located in chromosome 16 at position of 13.2. This gene goes by a number of names, including, GABA transaminase, GABAT, 4-aminobutyrate transaminase, NPD009 etc. This gene is mainly and abundant located in neuronal tissues. 4-Aminobutyrate aminotransferase belongs to group of pyridoxal 5-phosphate-dependent enzyme which activates a large portion giving reaction to amino acids. ABAT is made up of two monomers of enzymes where each subunit has a molecular weight of 50kDa. It is identified that almost tierce of human synapses have GABA. GABA is a neurotransmitter that has different roles in different regions of the central and peripheral nervous systems. It can be found also in some tissues that do not have neurons. In addition, GAD and GABA-AT are responsible in regulating the concentration of GABA.

<span class="mw-page-title-main">ACOT1</span> Protein-coding gene in the species Homo sapiens

Acyl-CoA thioesterase 1 is a protein that in humans is encoded by the ACOT1 gene.

References

  1. ↑ "Human Metabolome Database: Showing metabocard for Butyryl-CoA (HMDB0001088)".
  2. 1 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. ↑ 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.
  8. ↑ Haapalainen AM, Meriläinen G, Pirilä PL, Kondo N, Fukao T, Wierenga RK (2007-03-20). "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.
  9. ↑ 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.
  10. ↑ Stern JR, Coon MJ, Del Campillo A (1953-01-03). "Enzymatic breakdown and synthesis of acetoacetate". Nature. 171 (4340): 28–30. Bibcode:1953Natur.171...28S. doi:10.1038/171028a0. ISSN   0028-0836. PMID   13025466.
  11. ↑ Goldman DS (May 1954). "Studies on the fatty acid oxidizing system of animal tissues. VII. The beta-ketoacyl coenzyme A cleavage enzyme". The Journal of Biological Chemistry. 208 (1): 345–357. doi: 10.1016/S0021-9258(18)65653-4 . ISSN   0021-9258. PMID   13174544.
  12. 1 2 Campbell JW, Cronan JE (July 2002). "The Enigmatic Escherichia coli fadE Gene Is yafH". Journal of Bacteriology. 184 (13): 3759–3764. doi:10.1128/JB.184.13.3759-3764.2002. ISSN   0021-9193. PMC   135136 . PMID   12057976.
  13. ↑ Ikeda Y, Okamura-Ikeda K, Tanaka K (1985-01-25). "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". The Journal of Biological Chemistry. 260 (2): 1311–1325. doi: 10.1016/S0021-9258(20)71245-7 . ISSN   0021-9258. PMID   3968063.
  14. ↑ Matsubara Y, Indo Y, Naito E, Ozasa H, Glassberg R, Vockley J, et al. (1989-09-25). "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". The Journal of Biological Chemistry. 264 (27): 16321–16331. doi: 10.1016/S0021-9258(18)71624-4 . ISSN   0021-9258. PMID   2777793.
  15. ↑ Kim JJ, Wang M, Paschke R (1993-08-15). "Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate". Proceedings of the National Academy of Sciences. 90 (16): 7523–7527. Bibcode:1993PNAS...90.7523K. doi: 10.1073/pnas.90.16.7523 . ISSN   0027-8424. PMC   47174 . PMID   8356049.
  16. ↑ VANHOOREN JC, MARYNEN P, MANNAERTS GP, VAN VELDHOVEN PP (1997-08-01). "Evidence for the existence of a pristanoyl-CoA oxidase gene in man". Biochemical Journal. 325 (3): 593–599. doi:10.1042/bj3250593. ISSN   0264-6021. PMC   1218600 . PMID   9271077.
  17. ↑ Willard J, Vicanek C, Battaile KP, Van Veldhoven PP, Fauq AH, Rozen R, et al. (1996-07-01). "Cloning of a cDNA for Short/Branched Chain Acyl-Coenzyme A Dehydrogenase from Rat and Characterization of Its Tissue Expression and Substrate Specificity". Archives of Biochemistry and Biophysics. 331 (1): 127–133. doi:10.1006/abbi.1996.0290. ISSN   0003-9861. PMID   8660691.
  18. ↑ Barker HA, Kamen MD, Bornstein BT (December 1945). "The Synthesis of Butyric and Caproic Acids from Ethanol and Acetic Acid by Clostridium Kluyveri". Proceedings of the National Academy of Sciences. 31 (12): 373–381. Bibcode:1945PNAS...31..373B. doi: 10.1073/pnas.31.12.373 . ISSN   0027-8424. PMC   1078850 . PMID   16588706.
  19. 1 2 Bornstein BT, Barker HA (February 1948). "The energy metabolism of Clostridium kluyveri and the synthesis of fatty acids". The Journal of Biological Chemistry. 172 (2): 659–669. doi: 10.1016/S0021-9258(19)52752-1 . ISSN   0021-9258. PMID   18901185.
  20. 1 2 Kenealy WR, Waselefsky DM (April 1985). "Studies on the substrate range of Clostridium kluyveri; the use of propanol and succinate". Archives of Microbiology. 141 (3): 187–194. Bibcode:1985ArMic.141..187K. doi:10.1007/BF00408056. ISSN   0302-8933.
  21. ↑ Williamson G, Engel PC (1984-03-01). "Butyryl-CoA dehydrogenase from Megasphaera elsdenii . Specificity of the catalytic reaction". Biochemical Journal. 218 (2): 521–529. doi:10.1042/bj2180521. ISSN   0264-6021. PMC   1153368 . PMID   6712628.
  22. ↑ Turano FJ, Thakkar SS, Fang T, Weisemann JM (1997-04-01). "Characterization and Expression of NAD(H)-Dependent Glutamate Dehydrogenase Genes in Arabidopsis". Plant Physiology. 113 (4): 1329–1341. doi:10.1104/pp.113.4.1329. ISSN   1532-2548. PMC   158256 . PMID   9112779.
  23. ↑ Rangarajan ES, Li Y, Ajamian E, Iannuzzi P, Kernaghan SD, Fraser ME, et al. (December 2005). "Crystallographic Trapping of the Glutamyl-CoA Thioester Intermediate of Family I CoA Transferases". Journal of Biological Chemistry. 280 (52): 42919–42928. doi: 10.1074/jbc.M510522200 . PMID   16253988.
  24. ↑ 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.
  25. ↑ 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.
  26. 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.
  27. ↑ Hardman JK, Stadtman TC (April 1960). "METABOLISM OF ω-AMINO ACIDS: I. Fermentation of γ-Aminobutyric Acid by Clostridium aminobutyricum n. sp". Journal of Bacteriology. 79 (4): 544–548. doi:10.1128/jb.79.4.544-548.1960. ISSN   0021-9193. PMC   278728 . PMID   14399736.
  28. ↑ Hardman JK, Stadtman TC (June 1963). "Metabolism of amega-amino acids. III. Mechanism of conversion of gamma-aminobutyrate to gamma-hydroxybutryate by Clostridium aminobutyricum". The Journal of Biological Chemistry. 238 (6): 2081–2087. doi: 10.1016/S0021-9258(18)67943-8 . ISSN   0021-9258. PMID   13952769.
  29. ↑ Andersen G, Andersen B, Dobritzsch D, Schnackerz KD, Piškur J (April 2007). "A gene duplication led to specialized γ-aminobutyrate and β-alanine aminotransferase in yeast". The FEBS Journal. 274 (7): 1804–1817. doi:10.1111/j.1742-4658.2007.05729.x. ISSN   1742-464X. PMID   17355287.
  30. ↑ 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.
  31. ↑ Jakoby WB, Scott EM (April 1959). "Aldehyde oxidation. III. Succinic semialdehyde dehydrogenase". The Journal of Biological Chemistry. 234 (4): 937–940. doi: 10.1016/S0021-9258(18)70207-X . ISSN   0021-9258. PMID   13654295.
  32. ↑ Li K, Xu E (2008-06-01). "The role and the mechanism of γ-aminobutyric acid during central nervous system development". Neuroscience Bulletin. 24 (3): 195–200. doi:10.1007/s12264-008-0109-3. ISSN   1995-8218. PMC   5552538 . PMID   18500393.
  33. ↑ de Leon AS, Tadi P (2024), "Biochemistry, Gamma Aminobutyric Acid", StatPearls, Treasure Island (FL): StatPearls Publishing, PMID   31869147 , retrieved 2024-04-14
  34. ↑ Donahue MJ, Near J, Blicher JU, Jezzard P (2010-11-01). "Baseline GABA concentration and fMRI response". NeuroImage. 53 (2): 392–398. doi:10.1016/j.neuroimage.2010.07.017. ISSN   1053-8119. PMID   20633664.
  35. ↑ 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.
  36. ↑ 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.
  37. ↑ Wiesenborn DP, Rudolph FB, Papoutsakis ET (November 1988). "Thiolase from Clostridium acetobutylicum ATCC 824 and Its Role in the Synthesis of Acids and Solvents". Applied and Environmental Microbiology. 54 (11): 2717–2722. Bibcode:1988ApEnM..54.2717W. doi:10.1128/aem.54.11.2717-2722.1988. ISSN   0099-2240. PMC   204361 . PMID   16347774.
  38. ↑ Stabler SP, Marcell PD, Allen RH (August 1985). "Isolation and characterization of dl-methylmalonyl-coenzyme A racemase from rat liver". Archives of Biochemistry and Biophysics. 241 (1): 252–264. doi:10.1016/0003-9861(85)90381-9. PMID   2862845.
  39. ↑ 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.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.