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/Assimilation → Carboxylates 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
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
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
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
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
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
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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