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Chemical Compound Review

AG-H-90164     6-[[(1S)-3-[[(1S)-3- aminocarbonyl-1...

Synonyms: CTK5H6691, AC1L3TZ5, 94483-60-0
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Disease relevance of formyl-MFR


High impact information on formyl-MFR


Biological context of formyl-MFR


Associations of formyl-MFR with other chemical compounds


Gene context of formyl-MFR

  • Interestingly, these are encoded by the genes orf1, orf2 and orf3 which show sequence identity with the formylMFR dehydrogenase subunits FmdA, FmdB and FmdC, respectively [9].
  • The finding that FmdF forms a tight complex with the other subunits of formylmethanofuran dehydrogenase indicates a function of the polyferredoxin in the reaction catalyzed by the enzyme. fmdE encodes a protein not present in the purified enzyme [11].

Analytical, diagnostic and therapeutic context of formyl-MFR

  • The active form of formylmethanofuran dehydrogenase had an apparent molecular mass of 530 kDa as determined by gel filtration chromatography and was found to copurify with a hydrogenase [12].


  1. Primary structure and properties of the formyltransferase from the mesophilic Methanosarcina barkeri: comparison with the enzymes from thermophilic and hyperthermophilic methanogens. Kunow, J., Shima, S., Vorholt, J.A., Thauer, R.K. Arch. Microbiol. (1996) [Pubmed]
  2. The role of formylmethanofuran: tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide. Donnelly, M.I., Wolfe, R.S. J. Biol. Chem. (1986) [Pubmed]
  3. Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri. Shima, S., Thauer, R.K., Michel, H., Ermler, U. Proteins (1996) [Pubmed]
  4. Properties of the tungsten-substituted molybdenum formylmethanofuran dehydrogenase from Methanobacterium wolfei. Schmitz, R.A., Albracht, S.P., Thauer, R.K. FEBS Lett. (1992) [Pubmed]
  5. Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum (Marburg). Börner, G., Karrasch, M., Thauer, R.K. FEBS Lett. (1991) [Pubmed]
  6. Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanosarcina barkeri. Identification of N5-formyltetrahydromethanopterin as the product. Breitung, J., Thauer, R.K. FEBS Lett. (1990) [Pubmed]
  7. The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum. Structures and transcriptional regulation. Hochheimer, A., Linder, D., Thauer, R.K., Hedderich, R. Eur. J. Biochem. (1996) [Pubmed]
  8. Formylmethanofuran dehydrogenase from methanogenic bacteria, a molybdoenzyme. Karrasch, M., Börner, G., Enssle, M., Thauer, R.K. FEBS Lett. (1989) [Pubmed]
  9. Characterization of the formyltransferase from Methylobacterium extorquens AM1. Pomper, B.K., Vorholt, J.A. Eur. J. Biochem. (2001) [Pubmed]
  10. Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase. Bertram, P.A., Schmitz, R.A., Linder, D., Thauer, R.K. Arch. Microbiol. (1994) [Pubmed]
  11. A polyferredoxin with eight [4Fe-4S] clusters as a subunit of molybdenum formylmethanofuran dehydrogenase from Methanosarcina barkeri. Vorholt, J.A., Vaupel, M., Thauer, R.K. Eur. J. Biochem. (1996) [Pubmed]
  12. Formylmethanofuran synthesis by formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum Marburg. Wasserfallen, A. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
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