Abstract
Methanofuran involved in methanogenesis. The N-formyl derivative is an intermediate in the reduction of CO 2 to CH 4 and the disproportionation of methanol to CO 2 and CH 4. Formylmethanofuran dehydrogenase and formylmethanofuran:tetrahydromethanopterin formyltransferase are the enzymes catalyzing its conversions. We report here that the two enzymes from Methanosarcma barkeri and the formyltransferase from Methanobacterium thermoautotrophicum can also use N-furfurylfonnamide as a pseudo-substrate albeit with higher apparent K m and lower apparent V max values. N-Methylformamide, formamide, and formate were not converted indicating that the furfurylamine moiety of methanofuran is the minimum structure required for the correct binding of the coenzyme.
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