Methanol dissimilation in Xanthobacter H4-14: activities, induction and comparison to Pseudomonas AM1 and Paracoccus denitrificans.
Methanol dissimilatory enzymes detected in the methanol autotroph Xanthobacter 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 Paracoccus denitrificans, Xanthobacter H4-14, and Pseudomonas AM1. P. denitrificans contained a previously reported NAD+-linked, GSH-dependent activity, but both Xanthobacter H4-14 and Pseudomonas AM1 contained numerous activities detected by activity stains of polyacrylamide gels. Induction studies showed that in Xanthobacter H4-14, a 10 kDal polypeptide, probably a dehydrogenase-associated cytochrome c, was co-induced with methanol dehydrogenase, but the formaldehyde and formate dehydrogenases were not co-regulated. Analogous induction experiments revealed similar patterns in P. denitrificans, but no evidence for co-regulation of dissimilatory activities in Pseudomonas AM1.
Weaver
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Lidstrom
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D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000096:biosynthesis; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology* / Q000254:growth & development; D000432:Methanol / Q000378:metabolism*; D010231:Paracoccus denitrificans / Q000201:enzymology / Q000254:growth & development; D011549:Pseudomonas / Q000201:enzymology / Q000254:growth & development
D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; D000432:Methanol