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. 1972 May;110(2):570–577. doi: 10.1128/jb.110.2.570-577.1972

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

R N Patel a,1, H R Bose a, W J Mandy a, D S Hoare a,2
PMCID: PMC247450  PMID: 5022170

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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