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MetaCyc Pathway: acetate conversion to acetyl-CoA
Inferred from experiment

Enzyme View:

Pathway diagram: acetate conversion to acetyl-CoA

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Degradation/Utilization/AssimilationCarboxylates Degradation

Some taxa known to possess this pathway include : Cupriavidus necator, Escherichia coli K-12 substr. MG1655, Haloarcula marismortui, Halobacteria, Halococcus saccharolyticus, Haloferax volcanii, Halorubrum saccharovorum, Homo sapiens, Mammalia, Saccharomyces cerevisiae

Expected Taxonomic Range: Archaea, Bacteria , Opisthokonta

This pathway is widely spread, and is found in archaea, bacteria and eukarya.

When halophilic archaebacteria grow on glucose they form acetate which is excreted into the medium. This conversion is catalyzed by the enzyme acetate-CoA ligase (ADP-forming) (see acetate formation from acetyl-CoA II). In stationary phase the cells consume the excreted acetate, in a pathway that involves its conversion back to acetyl-CoA. This reverse reaction is not catalyzed by acetate-CoA ligase (ADP-forming), but by acetyl-CoA synthetase (AMP-forming) [Brasen01].

In yeasts, respiratory dissimilation of pyruvate is initiated by its conversion into acetyl-CoA, which occurs either a direct reaction catalyzed by the mitochondrial pyruvate dehydrogenase complex, or via an indirect route, involving pyruvate decarboxylase, acetaldehyde dehydrogenase and acetyl-coenzyme A synthetase [Holzer57, Pronk94].

Acetate plays multiple roles in the metabolism of Escherichia coli K-12. In the absence of other substrates acetate can serve as a total source of carbon and energy. The acs pathway (named after the acs gene, which encodes acetyl-CoA synthetase (AMP-forming) in this organism) is an inducible pathway that plays a major role in the aerobic utilization of acetate. Mutant strains blocked in the acs pathway grow poorly on acetate. Mutants blocked in both pathways are unable to grow on acetate. Because it is a high-affinity system, the acs pathway is the major scavenger of acetate when extracellular concentrations of it are low. It also enables Escherichia coli to utilize propanoate. Reviewed in Clark, D.P. and John E. Cronan. EcoSal module 3.4.4 [ECOSAL].

Superpathways: superpathway of acetate utilization and formation

Unification Links: EcoCyc:PWY0-1313

Created 31-Jul-2007 by Caspi R, SRI International


Brasen01: Brasen C, Schonheit P (2001). "Mechanisms of acetate formation and acetate activation in halophilic archaea." Arch Microbiol 175(5);360-8. PMID: 11409546

ECOSAL: EcoSal "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition.

Holzer57: Holzer, H., Goedde, H.W. (1957). "[Two ways from pyruvate to acetyl-coenzyme A in yeast.]." Biochem Z 329(3);175-91. PMID: 13522696

Pronk94: Pronk JT, Wenzel TJ, Luttik MA, Klaassen CC, Scheffers WA, Steensma HY, van Dijken JP (1994). "Energetic aspects of glucose metabolism in a pyruvate-dehydrogenase-negative mutant of Saccharomyces cerevisiae." Microbiology 140 ( Pt 3);601-10. PMID: 8012582

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Baeza14: Baeza J, Dowell JA, Smallegan MJ, Fan J, Amador-Noguez D, Khan Z, Denu JM (2014). "Stoichiometry of site-specific lysine acetylation in an entire proteome." J Biol Chem 289(31);21326-38. PMID: 24917678

Baptist13: Baptist G, Pinel C, Ranquet C, Izard J, Ropers D, de Jong H, Geiselmann J (2013). "A genome-wide screen for identifying all regulators of a target gene." Nucleic Acids Res 41(17);e164. PMID: 23892289

Barak01: Barak R, Eisenbach M (2001). "Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis." Mol Microbiol 40(3);731-43. PMID: 11359578

Barak04: Barak R, Eisenbach M (2004). "Co-regulation of acetylation and phosphorylation of CheY, a response regulator in chemotaxis of Escherichia coli." J Mol Biol 342(2);375-81. PMID: 15327941

Barak04a: Barak R, Prasad K, Shainskaya A, Wolfe AJ, Eisenbach M (2004). "Acetylation of the chemotaxis response regulator CheY by acetyl-CoA synthetase purified from Escherichia coli." J Mol Biol 342(2);383-401. PMID: 15327942

Barak06: Barak R, Yan J, Shainskaya A, Eisenbach M (2006). "The chemotaxis response regulator CheY can catalyze its own acetylation." J Mol Biol 359(2);251-65. PMID: 16630631

Barak92: Barak R, Welch M, Yanovsky A, Oosawa K, Eisenbach M (1992). "Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch." Biochemistry 31(41);10099-107. PMID: 1390767

Barak98: Barak R, Abouhamad WN, Eisenbach M (1998). "Both acetate kinase and acetyl coenzyme A synthetase are involved in acetate-stimulated change in the direction of flagellar rotation in Escherichia coli." J Bacteriol 1998;180(4);985-8. PMID: 9473056

Bernal14: Bernal V, Castano-Cerezo S, Gallego-Jara J, Ecija-Conesa A, de Diego T, Iborra JL, Canovas M (2014). "Regulation of bacterial physiology by lysine acetylation of proteins." N Biotechnol 31(6);586-95. PMID: 24636882

Brock02: Brock M, Maerker C, Schutz A, Volker U, Buckel W (2002). "Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase." Eur J Biochem 269(24);6184-94. PMID: 12473114

Brown77: Brown TD, Jones-Mortimer MC, Kornberg HL (1977). "The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli." J Gen Microbiol 1977;102(2);327-36. PMID: 21941

Canovas03: Canovas M, Bernal V, Torroglosa T, Ramirez JL, Iborra JL (2003). "Link between primary and secondary metabolism in the biotransformation of trimethylammonium compounds by escherichia coli." Biotechnol Bioeng 84(6);686-99. PMID: 14595781

CastanoCerezo09: Castano-Cerezo S, Pastor JM, Renilla S, Bernal V, Iborra JL, Canovas M (2009). "An insight into the role of phosphotransacetylase (pta) and the acetate/acetyl-CoA node in Escherichia coli." Microb Cell Fact 8;54. PMID: 19852855

CastanoCerezo11: Castano-Cerezo S, Bernal V, Blanco-Catala J, Iborra JL, Canovas M (2011). "cAMP-CRP co-ordinates the expression of the protein acetylation pathway with central metabolism in Escherichia coli." Mol Microbiol 82(5);1110-28. PMID: 22059728

CastanoCerezo14: Castano-Cerezo S, Bernal V, Post H, Fuhrer T, Cappadona S, Sanchez-Diaz NC, Sauer U, Heck AJ, Altelaar AF, Canovas M (2014). "Protein acetylation affects acetate metabolism, motility and acid stress response in Escherichia coli." Mol Syst Biol 10;762. PMID: 25518064

CastanoCerezo15: Castano-Cerezo S, Bernal V, Rohrig T, Termeer S, Canovas M (2015). "Regulation of acetate metabolism in Escherichia coli BL21 by protein N(ε)-lysine acetylation." Appl Microbiol Biotechnol 99(8);3533-45. PMID: 25524697

deDiego15: de Diego Puente T, Gallego-Jara J, Castano-Cerezo S, Bernal Sanchez V, Fernandez Espin V, Garcia de la Torre J, Manjon Rubio A, Canovas Diaz M (2015). "The Protein Acetyltransferase PatZ from Escherichia coli Is Regulated by Autoacetylation-induced Oligomerization." J Biol Chem 290(38);23077-93. PMID: 26251518

deJongGubbels97: de Jong-Gubbels P, van den Berg MA, Steensma HY, van Dijken JP, Pronk JT (1997). "The Saccharomyces cerevisiae acetyl-coenzyme A synthetase encoded by the ACS1 gene, but not the ACS2-encoded enzyme, is subject to glucose catabolite inactivation." FEMS Microbiol Lett 153(1);75-81. PMID: 9252575

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Esquerre14: Esquerre T, Laguerre S, Turlan C, Carpousis AJ, Girbal L, Cocaign-Bousquet M (2014). "Dual role of transcription and transcript stability in the regulation of gene expression in Escherichia coli cells cultured on glucose at different growth rates." Nucleic Acids Res 42(4);2460-72. PMID: 24243845

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sun May 1, 2016, biocyc14.