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Gene Review

acs  -  acetyl-CoA synthetase

Escherichia coli UTI89

 
 
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Disease relevance of acs

 

High impact information on acs

  • N- and C-terminal parts of the G. lamblia acetyl-CoA synthetase sequence were found to be homologous to the alpha- and beta-subunits, respectively, of succinyl-CoA synthetase [2].
  • Acetyl-CoA synthetase from the amitochondriate eukaryote Giardia lamblia belongs to the newly recognized superfamily of acyl-CoA synthetases (Nucleoside diphosphate-forming) [2].
  • Here, we used electrophoretic mobility shift assays and DNase I footprint analyses to demonstrate that the nucleoid proteins FIS and IHF each bind multiple sites within the acs regulatory region, that FIS competes successfully with CRP for binding to their overlapping and neighbouring sites and that IHF binds independently of either FIS or CRP [3].
  • These observations suggest that Acs-mediated acetylation of CheY is involved in chemotaxis and that the acetylation site Lys-92 is only involved in the response to repellents [4].
  • It is well established that the response regulator of the chemotaxis system of Escherichia coli, CheY, can undergo acetylation at lysine residues 92 and 109 via a reaction mediated by acetyl-CoA synthetase (Acs) [4].
 

Chemical compound and disease context of acs

 

Biological context of acs

  • The amino acid sequence deduced from the nucleotide sequence of the acs gene showed homology with those of functionally related proteins, i.e., proteins involved in the binding of coenzyme A, ATP, or both [7].
  • In all cases, the acetate-crossfeeding phenotype is associated with semiconstitutive overexpression of acetyl CoA synthetase, which allows for the enhanced uptake of low levels of exogenous acetate [8].
  • In addition, the presence of Acs elevated the phosphorylation levels of both CheA and CheY, and acetate repressed this stimulation [9].
  • Sirtuins are NAD+-dependent protein deacetylase enzymes that are broadly conserved from bacteria to human, and have been implicated to play important roles in gene regulation, metabolism and longevity. cobB is a bacterial sirtuin that deacetylates acetyl-CoA synthetase (Acs) at an active site lysine to stimulate its enzymatic activity [10].
  • As they begin the transition to stationary phase, they instead resorb acetate, activate it to acetyl coenzyme A (acetyl-CoA) by means of the enzyme acetyl-CoA synthetase (Acs) and utilize it to generate energy and biosynthetic components via the tricarboxylic acid cycle and the glyoxylate shunt, respectively [11].
 

Associations of acs with chemical compounds

  • The fortuitous presence of an IS2 element in acs, which impaired yjcG expression by polarity in our parental strain, allowed us to conclude that the alternative glycolate carrier became active after precise excision of IS2 in the suppressed strain [12].
  • As they begin the transition to stationary phase, they instead resorb acetate, activate it to acetyl coenzyme A (acetyl-CoA) by means of the enzyme acetyl-CoA synthetase (Acs) and utilize it to generate energy and biosynthetic components via the tricarboxylic acid cycle and the glyoxylate shunt, respectively [13].
  • ADP-forming acetyl-CoA synthetase (ACD), the novel enzyme of acetate formation and energy conservation in archaea Acety - CoA + ADP + Pi<==>acetate + ATP CoA), has been studied only in few hyperthermophilic euryarchaea [14].
  • 2D gel electrophoresis showed the production of all proteins encoded by the prp operon during growth on propionate as sole carbon and energy source, except PrpE, which seems to be replaced by acetyl-CoA synthetase [15].
  • Based on the investigation of enzyme activities and intracellular metabolite concentrations, acetyl-CoA was considered to be formed by the combined reactions through pyruvate oxidase (PoxB), acetyl-CoA synthetase (Acs) and acetate kinase (Ack)-phosphoacetyltransferase (Pta) in the lpdA mutant [16].
 

Analytical, diagnostic and therapeutic context of acs

  • By Western blotting with specific anti-acetyl-lysine antibody we demonstrated that Acs undergoes autoacetylation, that CheY is acetylated to a small extent when isolated, and that the extent is elevated following in vitro acetylation [17].

References

  1. The Escherichia coli K-12 NarL and NarP Proteins Insulate the nrf Promoter from the Effects of Integration Host Factor. Browning, D.F., Lee, D.J., Wolfe, A.J., Cole, J.A., Busby, S.J. J. Bacteriol. (2006) [Pubmed]
  2. Acetyl-CoA synthetase from the amitochondriate eukaryote Giardia lamblia belongs to the newly recognized superfamily of acyl-CoA synthetases (Nucleoside diphosphate-forming). Sánchez, L.B., Galperin, M.Y., Müller, M. J. Biol. Chem. (2000) [Pubmed]
  3. Modulation of CRP-dependent transcription at the Escherichia coli acsP2 promoter by nucleoprotein complexes: anti-activation by the nucleoid proteins FIS and IHF. Browning, D.F., Beatty, C.M., Sanstad, E.A., Gunn, K.E., Busby, S.J., Wolfe, A.J. Mol. Microbiol. (2004) [Pubmed]
  4. Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis. Barak, R., Eisenbach, M. Mol. Microbiol. (2001) [Pubmed]
  5. Glucose metabolism at high density growth of E. coli B and E. coli K: differences in metabolic pathways are responsible for efficient glucose utilization in E. coli B as determined by microarrays and Northern blot analyses. Phue, J.N., Noronha, S.B., Hattacharyya, R., Wolfe, A.J., Shiloach, J. Biotechnol. Bioeng. (2005) [Pubmed]
  6. Involvement of iclR and rpoS in the induction of acs, the gene for acetyl coenzyme A synthetase of Escherichia coli K-12. Shin, S., Song, S.G., Lee, D.S., Pan, J.G., Park, C. FEMS Microbiol. Lett. (1997) [Pubmed]
  7. Cloning, sequence analysis, and functional expression of the acetyl coenzyme A synthetase gene from Methanothrix soehngenii in Escherichia coli. Eggen, R.I., Geerling, A.C., Boshoven, A.B., de Vos, W.M. J. Bacteriol. (1991) [Pubmed]
  8. Repeated evolution of an acetate-crossfeeding polymorphism in long-term populations of Escherichia coli. Treves, D.S., Manning, S., Adams, J. Mol. Biol. Evol. (1998) [Pubmed]
  9. Co-regulation of acetylation and phosphorylation of CheY, a response regulator in chemotaxis of Escherichia coli. Barak, R., Eisenbach, M. J. Mol. Biol. (2004) [Pubmed]
  10. Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli. Zhao, K., Chai, X., Marmorstein, R. J. Mol. Biol. (2004) [Pubmed]
  11. Regulation of acetyl coenzyme A synthetase in Escherichia coli. Kumari, S., Beatty, C.M., Browning, D.F., Busby, S.J., Simel, E.J., Hovel-Miner, G., Wolfe, A.J. J. Bacteriol. (2000) [Pubmed]
  12. The gene yjcG, cotranscribed with the gene acs, encodes an acetate permease in Escherichia coli. Gimenez, R., Nuñez, M.F., Badia, J., Aguilar, J., Baldoma, L. J. Bacteriol. (2003) [Pubmed]
  13. sigma(70) is the principal sigma factor responsible for transcription of acs, which encodes acetyl coenzyme A synthetase in Escherichia coli. Kumari, S., Simel, E.J., Wolfe, A.J. J. Bacteriol. (2000) [Pubmed]
  14. Unusual ADP-forming acetyl-coenzyme A synthetases from the mesophilic halophilic euryarchaeon Haloarcula marismortui and from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. Bräsen, C., Schönheit, P. Arch. Microbiol. (2004) [Pubmed]
  15. Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Brock, M., Maerker, C., Schütz, A., Völker, U., Buckel, W. Eur. J. Biochem. (2002) [Pubmed]
  16. Effect of lpdA gene knockout on the metabolism in Escherichia coli based on enzyme activities, intracellular metabolite concentrations and metabolic flux analysis by 13C-labeling experiments. Li, M., Ho, P.Y., Yao, S., Shimizu, K. J. Biotechnol. (2006) [Pubmed]
  17. Acetylation of the chemotaxis response regulator CheY by acetyl-CoA synthetase purified from Escherichia coli. Barak, R., Prasad, K., Shainskaya, A., Wolfe, A.J., Eisenbach, M. J. Mol. Biol. (2004) [Pubmed]
 
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