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.
MeSH terms
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Alcohol Oxidoreductases* / isolation & purification
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Alcohol Oxidoreductases* / metabolism
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Bacteria / enzymology*
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Bacteria / metabolism
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Electrophoresis, Disc
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Ethidium
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Formaldehyde / metabolism
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Formates / biosynthesis
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Hydrogen-Ion Concentration
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Immunoelectrophoresis / drug effects
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Methane / metabolism*
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Methanol / metabolism*
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Molecular Weight
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Oxidation-Reduction
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Pseudomonas / enzymology*
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Pseudomonas / metabolism
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Species Specificity
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Spectrophotometry
Substances
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Formates
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Formaldehyde
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Alcohol Oxidoreductases
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Ethidium
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Methane
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Methanol