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A primary alcohol dehydrogenase has been purified fromMethylococcus 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 acidicp H. The enzyme is similar to an alcohol dehydrogenase enzyme isolated fromPseudomonas sp. M27.

journal of bacteriology

Physiological Studies of Methane- and Methanol-Oxidizing Bacteria: Comparison of a Primary Alcohol Dehydrogenase from <i>Methylococcus capsulatus</i> (Texas Strain) and <i>Pseudomonas</i> Species M27

Physiological Studies of Methane- and Methanol-Oxidizing Bacteria: Comparison of a Primary Alcohol Dehydrogenase from Methylococcus capsulatus (Texas Strain) and Pseudomonas Species M27