Summary: Methanol dissimilatory enzymes detected in the methanol autotroph H4-14 were a typical phenazine methosulphate-linked methanol dehydrogenase, a NAD-linked formate dehydrogenase, and a dye-linked formaldehyde dehydrogenase that could be assayed only by activity stains of polyacrylamide gels. This same methanol dehydrogenase activity was found in ethanol-grown cells and was apparently utilized for ethanol oxidation. Formaldehyde dehydrogenase activities were investigated in H4-14, and AM1. contained a previously reported NAD-linked, GSH-dependent activity, but both H4-14 and AM1 contained numerous activities detected by activity stains of polyacrylamide gels. Induction studies showed that in H4-14, a 10 kDal polypeptide, probably a dehydrogenase-associated cytochrome , was co-induced with methanol dehydrogenase, but the formaldehyde and formate dehydrogenases were not co-regulated. Analogous induction experiments revealed similar patterns in , but no evidence for co-regulation of dissimilatory activities in AM1.


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