Acetyl-CoA

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Acetyl-CoA
Acetyl-CoA-2D colored.svg
Names
IUPAC name
S-[2-[3-[[(2R)-4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanoyl]amino]propanoylamino]ethyl] ethanethioate
Identifiers
3D model (JSmol)
ChEBI
ChemSpider
ECHA InfoCard 100.000.719
KEGG
MeSH Acetyl+Coenzyme+A
Properties
C23H38N7O17P3S
Molar mass 809.57 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
N verify (what is YesYN ?)
Infobox references

Acetyl coenzyme A or acetyl-CoA is a molecule that participates in many biochemical reactions in protein, carbohydrate and lipid metabolism.[1] Its main function is to deliver the acetyl group to the citric acid cycle (Krebs cycle) to be oxidized for energy production. Coenzyme A (CoASH or CoA) consists of a β-mercaptoethylamine group linked to the vitamin pantothenic acid through an amide linkage [2] and 3'-phosphorylated ADP. The acetyl group (indicated in blue in the structural diagram on the right) of acetyl-CoA is linked to the sulfhydryl substituent of the β-mercaptoethylamine group, this thioester linkage is a "high energy" bond, which is particularly reactive. Hydrolysis of the thioester bond is exergonic (−31.5 kJ/mol).

CoA is acetylated to acetyl-CoA by the breakdown of carbohydrates through glycolysis and by the breakdown of fatty acids through β-oxidation. Acetyl-CoA then enters the citric acid cycle, where the acetyl group is oxidized to carbon dioxide and water, and the energy released captured in the form of 11 ATP and one GTP per acetyl group.

Konrad Bloch and Feodor Lynen were awarded the 1964 Nobel Prize in Physiology and Medicine for their discoveries linking acetyl-CoA and fatty acid metabolism. Fritz Lipmann won the Nobel Prize in 1953 for his discovery of the cofactor coenzyme A.

Direct synthesis[edit]

The acetylation of CoA is determined by the carbon sources.[3][4]

Extramitochondrial[edit]

Intramitochondrial[edit]

Pyruvate dehydrogenase complex reaction
  • At high glucose levels, acetyl-CoA is produced through glycolysis.[10] Pyruvate undergoes oxidative decarboxylation in which it loses its carboxyl group (as carbon dioxide) to form acetyl-CoA, giving off 33.5 kJ/mol of energy. The oxidative conversion of pyruvate into acetyl-CoA is referred to as the pyruvate dehydrogenase reaction. It is catalyzed by the pyruvate dehydrogenase complex. Other conversions between pyruvate and acetyl-CoA are possible, for example, pyruvate formate lyase disproportionates pyruvate into acetyl-CoA and formic acid.

Functions[edit]

Intermediates in various pathways[edit]

Interactive pathway map[edit]

Click on genes, proteins and metabolites below to visit Gene Wiki pages and related Wikipedia articles. The pathway can be downloaded and edited at WikiPathways.

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See also[edit]

References[edit]

  1. ^ "Acetyl CoA Crossroads". chemistry.elmhurst.edu. Retrieved 2016-11-08. 
  2. ^ "Fatty Acids -- Structure of Acetyl CoA". library.med.utah.edu. Retrieved 2017-06-02. 
  3. ^ Hynes, Michael J.; Murray, Sandra L. (2010-07-01). "ATP-Citrate Lyase Is Required for Production of Cytosolic Acetyl Coenzyme A and Development in Aspergillus nidulans". Eukaryotic Cell. 9 (7): 1039–1048. doi:10.1128/EC.00080-10. ISSN 1535-9778. PMC 2901662Freely accessible. PMID 20495057. 
  4. ^ Wellen, Kathryn E.; Thompson, Craig B. (2012-04-01). "A two-way street: reciprocal regulation of metabolism and signalling". Nature Reviews Molecular Cell Biology. 13 (4): 270–276. doi:10.1038/nrm3305. ISSN 1471-0072. PMID 22395772. 
  5. ^ Storey, Kenneth B. (2005-02-25). Functional Metabolism: Regulation and Adaptation. John Wiley & Sons. ISBN 9780471675570. 
  6. ^ "ACLY ATP citrate lyase [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-11-06. 
  7. ^ Ragsdale, S. W. (2004). "Life with carbon monoxide". CRC Critical Reviews in Biochemistry and Molecular Biology. 39: 165–195. 
  8. ^ Chatterjea (2004-01-01). Textbook of Biochemistry for Dental/Nursing/Pharmacy Students. Jaypee Brothers Publishers. ISBN 9788180612046. 
  9. ^ a b Berg, Jeremy M.; Tymoczko, John L.; Stryer, Lubert (2002). Biochemistry (5th ed.). W. H. Freeman. ISBN 0716730510. 
  10. ^ Blackstock, James C. (2014-06-28). Guide to Biochemistry. Butterworth-Heinemann. ISBN 9781483183671. 
  11. ^ Houten, Sander Michel; Wanders, Ronald J. A. (2010-03-02). "A general introduction to the biochemistry of mitochondrial fatty acid β-oxidation". Journal of Inherited Metabolic Disease. 33 (5): 469–477. doi:10.1007/s10545-010-9061-2. ISSN 0141-8955. PMC 2950079Freely accessible. PMID 20195903. 
  12. ^ a b c d e f g Stryer, Lubert (1995). Biochemistry (Fourth ed.). New York: W.H. Freeman and Company. pp. 510–515, 559–565, 581–613, 614–623, 775–778. ISBN 0-7167-2009-4. 
  13. ^ "Oxidation of fatty acids". 
  14. ^ "Ketone body metabolism". University of Waterloo. 
  15. ^ a b Ferre, P.; F. Foufelle (2007). "SREBP-1c Transcription Factor and Lipid Homeostasis: Clinical Perspective". Hormone Research. 68 (2): 72–82. doi:10.1159/000100426. PMID 17344645. Retrieved 2010-08-30. this process is outlined graphically in page 73 
  16. ^ a b Voet, Donald; Judith G. Voet; Charlotte W. Pratt (2006). Fundamentals of Biochemistry, 2nd Edition. John Wiley and Sons, Inc. pp. 547, 556. ISBN 0-471-21495-7. 
  17. ^ Fatland, B. L. (2005). "Reverse Genetic Characterization of Cytosolic Acetyl-CoA Generation by ATP-Citrate Lyase in Arabidopsis". The Plant Cell Online. 17: 182–203. doi:10.1105/tpc.104.026211. 
  18. ^ Yi, C. H.; Vakifahmetoglu-Norberg, H.; Yuan, J. (2011-01-01). "Integration of Apoptosis and Metabolism". Cold Spring Harbor Symposia on Quantitative Biology. 76: 375–387. doi:10.1101/sqb.2011.76.010777. ISSN 0091-7451. PMID 22089928. 
  19. ^ Pettit, Flora H.; Pelley, John W.; Reed, Lester J. (1975-07-22). "Regulation of pyruvate dehydrogenase kinase and phosphatase by acetyl-CoA/CoA and NADH/NAD ratios". Biochemical and Biophysical Research Communications. 65 (2): 575–582. doi:10.1016/S0006-291X(75)80185-9. 
  20. ^ Jitrapakdee, Sarawut; Maurice, Martin St.; Rayment, Ivan; Cleland, W. Wallace; Wallace, John C.; Attwood, Paul V. (2008-08-01). "Structure, Mechanism and Regulation of Pyruvate Carboxylase". The Biochemical Journal. 413 (3): 369–387. doi:10.1042/BJ20080709. ISSN 0264-6021. PMC 2859305Freely accessible. PMID 18613815. 

External links[edit]