Physiological studies of methane- and methanol-oxidizing bacteria: comparison of a primary alcohol dehydrogenase from Methylococcus capsulatus (Texas strain) and Pseudomonas species M27.

Journal of bacteriology ·Vol. 110 ·No. 2 ·1972-05-00 ·Pages 570-7

Patel RN, Bose HR, Mandy WJ, Hoare DS

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

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

Chemicals

Formates Formaldehyde Alcohol Oxidoreductases Ethidium Methane Methanol

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Patel R N

Bose H R

Mandy W J

Hoare D S

References (12)

12 references, click to expand

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Article Info

Journal

Journal of bacteriology

Abbr.

J Bacteriol

ISSN

0021-9193

DOI

10.1128/jb.110.2.570-577.1972

Published

1972-05-00

Pages

570-7

Language

English

Region

United States

NLM ID

2985120R

PMCID

PMC247450

Subset

External Links

PubMed source DOI: 10.1128/jb.110.2.570-577.1972 PMC Full Text View journal details

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Physiological studies of methane- and methanol-oxidizing bacteria: comparison of a primary alcohol dehydrogenase from Methylococcus capsulatus (Texas strain) and Pseudomonas species M27.

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