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J Bacteriol. 1972 May; 110(2): 570-577
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

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

^a Department of Microbiology, The University of Texas at Austin, Austin, Texas 78712

ABSTRACT

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.

¹ Present address: Department of Biology, Yale University, New Haven, Connecticut 06520.

² Deceased 16 May 1971.

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