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Gene Review

aceF  -  dihydrolipoamide acetyltransferase

Escherichia coli UTI89

 
 
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Disease relevance of aceF

 

High impact information on aceF

  • A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct [3].
  • A site-directed mutagenesis of this shortened aceF gene was carried out to replace the glutamine residue at position 291 (wild-type numbering) with a histidine residue [4].
  • Pirin regulates pyruvate catabolism by interacting with the pyruvate dehydrogenase e1 subunit and modulating pyruvate dehydrogenase activity [5].
  • The results support the view that synthesis of the PDH complex is regulated from the pdhR promoter of a pdhR-aceEF-lpd operon [6].
  • Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution [7].
 

Chemical compound and disease context of aceF

 

Biological context of aceF

  • The aceF gene comprises 1887 base pairs (629 codons excluding the initiation codon AUG); it is preceded by a short intercistronic segment of 14 base pairs containing a good ribosomal binding site, and it is followed closely by a potential rho-independent terminator [10].
 

Analytical, diagnostic and therapeutic context of aceF

  • In vitro deletion and site-directed mutagenesis of the aceF gene of Escherichia coli was used to generate dihydrolipoamide acetyltransferase (E2p) polypeptide chains containing various permutations and combinations of functional and non-functional lipoyl domains [11].
  • Protein pull-down and bacterial two-hybrid assays followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and electrospray ionization-tandem mass spectrometry analyses showed the pyruvate dehydrogenase (PDH) E1 subunit as a component interacting with the pirin(Sm) gene [5].

References

  1. Cloning of the aceF gene encoding the phosphomannose isomerase and GDP-mannose pyrophosphorylase activities involved in acetan biosynthesis in Acetobacter xylinum. Griffin, A.M., Poelwijk, E.S., Morris, V.J., Gasson, M.J. FEMS Microbiol. Lett. (1997) [Pubmed]
  2. Serum reactivity against bacterial pyruvate dehydrogenase: Increasing the specificity of anti-mitochondrial antibodies for the diagnosis of primary biliary cirrhosis. Miyakawa, H., Tanaka, A., Selmi, C., Hosoya, N., Mataki, N., Kikuchi, K., Kato, T., Arai, J., Goto, T., Gershwin, M.E. Clin. Dev. Immunol. (2006) [Pubmed]
  3. A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. Arjunan, P., Sax, M., Brunskill, A., Chandrasekhar, K., Nemeria, N., Zhang, S., Jordan, F., Furey, W. J. Biol. Chem. (2006) [Pubmed]
  4. Site-directed mutagenesis and 1H NMR spectroscopy of an interdomain segment in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Texter, F.L., Radford, S.E., Laue, E.D., Perham, R.N., Miles, J.S., Guest, J.R. Biochemistry (1988) [Pubmed]
  5. Pirin regulates pyruvate catabolism by interacting with the pyruvate dehydrogenase e1 subunit and modulating pyruvate dehydrogenase activity. Soo, P.C., Horng, Y.T., Lai, M.J., Wei, J.R., Hsieh, S.C., Chang, Y.L., Tsai, Y.H., Lai, H.C. J. Bacteriol. (2007) [Pubmed]
  6. A mutation causing constitutive synthesis of the pyruvate dehydrogenase complex in Escherichia coli is located within the pdhR gene. Haydon, D.J., Quail, M.A., Guest, J.R. FEBS Lett. (1993) [Pubmed]
  7. Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution. Chandrasekhar, K., Arjunan, P., Sax, M., Nemeria, N., Jordan, F., Furey, W. Acta Crystallogr. D Biol. Crystallogr. (2006) [Pubmed]
  8. Aerobic production of alanine by Escherichia coli aceF ldhA mutants expressing the Bacillus sphaericus alaD gene. Lee, M., Smith, G.M., Eiteman, M.A., Altman, E. Appl. Microbiol. Biotechnol. (2004) [Pubmed]
  9. Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complex. Nemeria, N.S., Korotchkina, L.G., Chakraborty, S., Patel, M.S., Jordan, F. Bioorg. Chem. (2006) [Pubmed]
  10. The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component. Stephens, P.E., Darlison, M.G., Lewis, H.M., Guest, J.R. Eur. J. Biochem. (1983) [Pubmed]
  11. Reductive acetylation of tandemly repeated lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli is random order. Allen, A.G., Perham, R.N., Allison, N., Miles, J.S., Guest, J.R. J. Mol. Biol. (1989) [Pubmed]
 
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