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MeSH Review

Methanosarcinaceae

 
 
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Disease relevance of Methanosarcinaceae

  • Cloning, sequence analysis, and functional expression of the acetyl coenzyme A synthetase gene from Methanothrix soehngenii in Escherichia coli [1].
  • The R. rubrum CODH is 67% similar to the beta subunit of the Clostridium thermoaceticum CODH and 47% similar to the alpha subunit of the Methanothrix soehngenii CODH; an alignment of these three peptides shows relatively limited overall conservation [2].
  • In contrast with the carbon monoxide dehydrogenases from most other anaerobic bacteria, the purified enzyme of Methanothrix soehngenii was remarkably stable towards oxygen and it was only slightly inhibited by cyanide [3].
 

High impact information on Methanosarcinaceae

 

Biological context of Methanosarcinaceae

 

Associations of Methanosarcinaceae with chemical compounds

 

Gene context of Methanosarcinaceae

  • This protein immunoreacted with antiserum raised against purified Acs isolated from an unrelated species, Methanothrix soehngenii [14].
  • Due to their presumed importance in removing cold-stabilised secondary structures in mRNA, we have characterised a putative DEAD-box RNA helicase gene (deaD) from the Antarctic methanogen, Methanococcoides burtonii [7].
  • Membrane ATPase from the aceticlastic methanogen Methanothrix thermophila [15].
  • The kinetic properties of the acetyl-CoA synthetase can explain the high affinity for acetate of Methanothrix soehngenii [10].
  • In the acetoclastic methanogen Methanothrix soehngenii, acetate is activated to acetyl coenzyme A by acetyl coenzyme A synthetase (Acs) [1].

References

  1. 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]
  2. Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system. Kerby, R.L., Hong, S.S., Ensign, S.A., Coppoc, L.J., Ludden, P.W., Roberts, G.P. J. Bacteriol. (1992) [Pubmed]
  3. Purification and characterization of an oxygen-stable carbon monoxide dehydrogenase of Methanothrix soehngenii. Jetten, M.S., Stams, A.J., Zehnder, A.J. Eur. J. Biochem. (1989) [Pubmed]
  4. The direct genetic encoding of pyrrolysine. Krzycki, J.A. Curr. Opin. Microbiol. (2005) [Pubmed]
  5. Cloning, expression, and sequence analysis of the genes for carbon monoxide dehydrogenase of Methanothrix soehngenii. Eggen, R.I., Geerling, A.C., Jetten, M.S., de Vos, W.M. J. Biol. Chem. (1991) [Pubmed]
  6. Primary structure of the chromosomal proteins MC1a, MC1b, and MC1c from the archaebacterium Methanothrix soehngenii. Chartier, F., Laine, B., Bélaïche, D., Sautière, P. J. Biol. Chem. (1989) [Pubmed]
  7. Low temperature regulated DEAD-box RNA helicase from the Antarctic archaeon, Methanococcoides burtonii. Lim, J., Thomas, T., Cavicchioli, R. J. Mol. Biol. (2000) [Pubmed]
  8. Structures of minor ether lipids isolated from the aceticlastic methanogen, Methanothrix concilii GP6. Ferrante, G., Brisson, J.R., Patel, G.B., Ekiel, I., Sprott, G.D. J. Lipid Res. (1989) [Pubmed]
  9. Methanogen diversity evidenced by molecular characterization of methyl coenzyme M reductase A (mcrA) genes in hydrothermal sediments of the Guaymas Basin. Dhillon, A., Lever, M., Lloyd, K.G., Albert, D.B., Sogin, M.L., Teske, A. Appl. Environ. Microbiol. (2005) [Pubmed]
  10. Isolation and characterization of acetyl-coenzyme A synthetase from Methanothrix soehngenii. Jetten, M.S., Stams, A.J., Zehnder, A.J. J. Bacteriol. (1989) [Pubmed]
  11. Partial gene sequences for the A subunit of methyl-coenzyme M reductase (mcrI) as a phylogenetic tool for the family Methanosarcinaceae. Springer, E., Sachs, M.S., Woese, C.R., Boone, D.R. Int. J. Syst. Bacteriol. (1995) [Pubmed]
  12. Acetate and CO2 assimilation by Methanothrix concilii. Ekiel, I., Sprott, G.D., Patel, G.B. J. Bacteriol. (1985) [Pubmed]
  13. Bacteriological composition and structure of granular sludge adapted to different substrates. Grotenhuis, J.T., Smit, M., Plugge, C.M., Xu, Y.S., van Lammeren, A.A., Stams, A.J., Zehnder, A.J. Appl. Environ. Microbiol. (1991) [Pubmed]
  14. Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli. Kumari, S., Tishel, R., Eisenbach, M., Wolfe, A.J. J. Bacteriol. (1995) [Pubmed]
  15. Membrane ATPase from the aceticlastic methanogen Methanothrix thermophila. Inatomi, K., Kamagata, Y., Nakamura, K. J. Bacteriol. (1993) [Pubmed]
 
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