Physiological studies of methane- and methanol-oxidizing bacteria: comparison of a primary alcohol dehydrogenase from Methylococcus capsulatus (Texas strain) and Pseudomonas species M27.
A primary alcohol dehydrogenase has been purified from Methylococcus capsulatus (Texas strain). The purified enzyme catalyzes the oxidation of methanol and formaldehyde to formate; other primary alcohols are oxidized to their corresponding aldehydes. Ammonium ions are required for enzyme activity. The enzyme has a molecular weight of 120,000 daltons and consists of two 62,000 molecular-weight subunits which dissociate at acidic pH. The enzyme is similar to an alcohol dehydrogenase enzyme isolated from Pseudomonas sp. M27.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology* / Q000378:metabolism; D004589:Electrophoresis, Disc; D004996:Ethidium; D005557:Formaldehyde / Q000378:metabolism; D005561:Formates / Q000096:biosynthesis; D006863:Hydrogen-Ion Concentration; D007122:Immunoelectrophoresis / Q000187:drug effects; D008697:Methane / Q000378:metabolism*; D000432:Methanol / Q000378:metabolism*; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011549:Pseudomonas / Q000201:enzymology* / Q000378:metabolism; D013045:Species Specificity; D013053:Spectrophotometry
D005561:Formates; D005557:Formaldehyde; D000429:Alcohol Oxidoreductases; D004996:Ethidium; D008697:Methane; D000432:Methanol