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 acetyl-CoA synthetase (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 acetyl-CoA synthetase (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
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
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
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
Gonidakis10: Gonidakis S, Finkel SE, Longo VD (2010). "E. coli hypoxia-inducible factor ArcA mediates lifespan extension in a lipoic acid synthase mutant by suppressing acetyl-CoA synthetase." Biol Chem 391(10);1139-47. PMID: 20707605
Gonidakis10a: Gonidakis S, Finkel SE, Longo VD (2010). "Genome-wide screen identifies Escherichia coli TCA-cycle-related mutants with extended chronological lifespan dependent on acetate metabolism and the hypoxia-inducible transcription factor ArcA." Aging Cell 9(5);868-81. PMID: 20707865
Kinnersley09: Kinnersley MA, Holben WE, Rosenzweig F (2009). "E Unibus Plurum: genomic analysis of an experimentally evolved polymorphism in Escherichia coli." PLoS Genet 5(11);e1000713. PMID: 19893610
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