1887

Abstract

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 AMI. contained a previously reported NAD-linked, GSH-dependent activity, but both H4-14 and AMI 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 AMI.

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/content/journal/micro/10.1099/00221287-131-9-2183
1985-09-01
2019-10-16
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-131-9-2183
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