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Chemical Compound Review

methyl-CoM     2-methylsulfanylethanesulfonic acid

Synonyms: Methyl com, AG-K-50142, CHEBI:17827, AC1Q6XAG, CTK4J8247, ...
 
 
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Disease relevance of methylcoenzyme M

 

High impact information on methylcoenzyme M

 

Biological context of methylcoenzyme M

 

Anatomical context of methylcoenzyme M

  • Membrane preparations produced from lysis of protoplasts or by sonication of whole cells gave comparatively low rates of methanogenesis (methylcoenzyme M methylreductase activity, less than or equal to 100 nmol of CH4 min-1 mg of protein-1), and no coupling with ATP synthesis could be demonstrated [12].
  • Without membranes, per mol of HCHO oxidized 1 mol H2 was formed and 1 mol CH4 was produced from CH3-CoM; the rate was 10-20% of that in the presence of membranes [13].
 

Associations of methylcoenzyme M with other chemical compounds

 

Gene context of methylcoenzyme M

  • We report here on experiments with methyl-coenzyme M analogues showing how they affect the activity and the MCR-red1 signal of MCR from Methanothermobacter marburgensis [14].
  • Upon addition of methyl-coenzyme M, the red2 signal disappeared and the red1 signal increased again [19].
  • The two fens had very similar diversity of methanogenic methyl-coenzyme M reductase gene (mcrA), but in the upper layer of the bog the methanogen diversity was strikingly lower, and only one type of mcrA sequence was retrieved [20].
  • The two polypeptides encoded by the open reading frames ORF1 and ORF2 of the methyl-CoM reductase transcription unit did not co-purify with the alpha, beta and gamma subunits [21].
 

Analytical, diagnostic and therapeutic context of methylcoenzyme M

References

  1. Enzyme-catalyzed methyl transfers to thiols: the role of zinc. Matthews, R.G., Goulding, C.W. Current opinion in chemical biology. (1997) [Pubmed]
  2. Structure of component B (7-mercaptoheptanoylthreonine phosphate) of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum. Noll, K.M., Rinehart, K.L., Tanner, R.S., Wolfe, R.S. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  3. The biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase. Selmer, T., Kahnt, J., Goubeaud, M., Shima, S., Grabarse, W., Ermler, U., Thauer, R.K. J. Biol. Chem. (2000) [Pubmed]
  4. X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation. Tang, Q., Carrington, P.E., Horng, Y.C., Maroney, M.J., Ragsdale, S.W., Bocian, D.F. J. Am. Chem. Soc. (2002) [Pubmed]
  5. Mechanistic studies of methane biogenesis by methyl-coenzyme M reductase: evidence that coenzyme B participates in cleaving the C-S bond of methyl-coenzyme M. Horng, Y.C., Becker, D.F., Ragsdale, S.W. Biochemistry (2001) [Pubmed]
  6. Methanol-dependent gene expression demonstrates that methyl-coenzyme M reductase is essential in Methanosarcina acetivorans C2A and allows isolation of mutants with defects in regulation of the methanol utilization pathway. Rother, M., Boccazzi, P., Bose, A., Pritchett, M.A., Metcalf, W.W. J. Bacteriol. (2005) [Pubmed]
  7. Component A2 of methylcoenzyme M reductase system from Methanobacterium thermoautotrophicum delta H: nucleotide sequence and functional expression by Escherichia coli. Kuhner, C.H., Lindenbach, B.D., Wolfe, R.S. J. Bacteriol. (1993) [Pubmed]
  8. Molecular analyses of methyl-coenzyme M reductase alpha-subunit (mcrA) genes in rice field soil and enrichment cultures reveal the methanogenic phenotype of a novel archaeal lineage. Lueders, T., Chin, K.J., Conrad, R., Friedrich, M. Environ. Microbiol. (2001) [Pubmed]
  9. Transport of coenzyme M (2-mercaptoethanesulfonic acid) and methylcoenzyme M [(2-methylthio)ethanesulfonic acid] in Methanococcus voltae: identification of specific and general uptake systems. Dybas, M., Konisky, J. J. Bacteriol. (1989) [Pubmed]
  10. Coenzyme M methylase activity of the 480-kilodalton corrinoid protein from Methanosarcina barkeri. Tallant, T.C., Krzycki, J.A. J. Bacteriol. (1996) [Pubmed]
  11. Methyl-coenzyme M reductase and other enzymes involved in methanogenesis from CO2 and H2 in the extreme thermophile Methanopyrus kandleri. Rospert, S., Breitung, J., Ma, K., Schwörer, B., Zirngibl, C., Thauer, R.K., Linder, D., Huber, R., Stetter, K.O. Arch. Microbiol. (1991) [Pubmed]
  12. Methanogenesis and ATP synthesis in a protoplast system of Methanobacterium thermoautotrophicum. Mountfort, D.O., Mörschel, E., Beimborn, D.B., Schönheit, P. J. Bacteriol. (1986) [Pubmed]
  13. Dependence on membrane components of methanogenesis from methyl-CoM with formaldehyde or molecular hydrogen as electron donors. Deppenmeier, U., Blaut, M., Gottschalk, G. Eur. J. Biochem. (1989) [Pubmed]
  14. Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues. Goenrich, M., Mahlert, F., Duin, E.C., Bauer, C., Jaun, B., Thauer, R.K. J. Biol. Inorg. Chem. (2004) [Pubmed]
  15. Formaldehyde oxidation and methanogenesis. Escalante-Semerena, J.C., Wolfe, R.S. J. Bacteriol. (1984) [Pubmed]
  16. EPR characterization of a high-spin system in carbon monoxide dehydrogenase from Methanothrix soehngenii. Jetten, M.S., Pierik, A.J., Hagen, W.R. Eur. J. Biochem. (1991) [Pubmed]
  17. Inorganic pyrophosphate synthesis during methanogenesis from methylcoenzyme M by cell-free extracts of Methanobacterium thermoautotrophicum (strain delta H). Keltjens, J.T., van Erp, R., Mooijaart, R.J., van der Drift, C., Vogels, G.D. Eur. J. Biochem. (1988) [Pubmed]
  18. Substrate-analogue-induced changes in the nickel-EPR spectrum of active methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum. Rospert, S., Voges, M., Berkessel, A., Albracht, S.P., Thauer, R.K. Eur. J. Biochem. (1992) [Pubmed]
  19. The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states. Mahlert, F., Grabarse, W., Kahnt, J., Thauer, R.K., Duin, E.C. J. Biol. Inorg. Chem. (2002) [Pubmed]
  20. Methanogen communities and Bacteria along an ecohydrological gradient in a northern raised bog complex. Juottonen, H., Galand, P.E., Tuittila, E.S., Laine, J., Fritze, H., Yrjälä, K. Environ. Microbiol. (2005) [Pubmed]
  21. Methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum (strain Marburg). Purity, activity and novel inhibitors. Ellermann, J., Rospert, S., Thauer, R.K., Bokranz, M., Klein, A., Voges, M., Berkessel, A. Eur. J. Biochem. (1989) [Pubmed]
  22. Component A2 of the methylcoenzyme M methylreductase system from Methanobacterium thermoautotrophicum. Rouvière, P.E., Escalante-Semerena, J.C., Wolfe, R.S. J. Bacteriol. (1985) [Pubmed]
  23. A methyl-CoM methylreductase system from methanogenic bacterium strain Gö 1 not requiring ATP for activity. Deppenmeier, U., Blaut, M., Jussofie, A., Gottschalk, G. FEBS Lett. (1988) [Pubmed]
  24. Evaluation of PCR amplification bias by terminal restriction fragment length polymorphism analysis of small-subunit rRNA and mcrA genes by using defined template mixtures of methanogenic pure cultures and soil DNA extracts. Lueders, T., Friedrich, M.W. Appl. Environ. Microbiol. (2003) [Pubmed]
  25. Tetrahydromethanopterin methyltransferase, a component of the methane synthesizing complex of Methanobacterium thermoautotrophicum. Sauer, F.D. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
 
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