Physiological regulation of Paracoccus denitrificans methanol dehydrogenase synthesis and activity.
An enzyme-linked immunosorbent assay and a whole-cell activity assay were developed which allowed detection of methanol dehydrogenase (MDH) of Paracoccus denitrificans with increased sensitivity. By these methods, it was shown that MDH was not induced by its natural substrate, methanol. Relief from a catabolite repression-like mechanism seemed responsible for low-level MDH synthesis, while product induction was the hypothesized mechanism for synthesis of high amounts of MDH. In the latter process, formaldehyde may play an important role as effector. For a variety of culture conditions, inconsistencies were observed in the relation between amounts of MDH protein synthesized and enzyme activities measured in vitro. Regulation of pyrrolo-quinoline-quinone biosynthesis or a modulation of its incorporation and stability in MDH may constitute an overriding mechanism to ensure a correct tuning between metabolic rates of methanol consumption and the required methanol oxidation rates.
D000429:Alcohol Oxidoreductases / Q000096:biosynthesis* / Q000378:metabolism; D004790:Enzyme Induction; D004797:Enzyme-Linked Immunosorbent Assay; D005557:Formaldehyde / Q000096:biosynthesis / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D007123:Immunoelectrophoresis, Two-Dimensional; D000432:Methanol / Q000378:metabolism; D010231:Paracoccus denitrificans / Q000201:enzymology*
D005557:Formaldehyde; D000429:Alcohol Oxidoreductases; C019641:alcohol dehydrogenase (acceptor); D005947:Glucose; D000432:Methanol