Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

AC1L975B 6-[[(1R)-3-[[(1R)-3-[2-[4- [[5...

Synonyms:

Jones, W.J. et al., Acharya, P. et al., Bobik, T.A. et al.

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High impact information on C00862

Methanofuran, characterized for the first time in an enzyme structure, is embedded in an elongated cleft at the homodimer interface and fixed by multiple hydrophobic interactions [1].
The roles of methanofuran and tetrahydromethanopterin as carriers of C1 moieties in the reduction of carbon dioxide to methane were studied in representatives of diverse groups of methanogens, confirming that these roles, first reported for Methanobacterium thermoautotrophicum, are common for methanogenesis in general [2].
Cell extracts prepared from cells of Methanosarcina barkeri grown on hydrogen and carbon dioxide, acetate, or methanol contain a coenzyme structurally related to methanofuran [3].

References

The structure of formylmethanofuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes. Acharya, P., Warkentin, E., Ermler, U., Thauer, R.K., Shima, S. J. Mol. Biol. (2006) [Pubmed]
Evidence of a common pathway of carbon dioxide reduction to methane in methanogens. Jones, W.J., Donnelly, M.I., Wolfe, R.S. J. Bacteriol. (1985) [Pubmed]
Structure of a methanofuran derivative found in cell extracts of Methanosarcina barkeri. Bobik, T.A., Donnelly, M.I., Rinehart, K.L., Wolfe, R.S. Arch. Biochem. Biophys. (1987) [Pubmed]

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