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

R. N. Patel | Zendy; Henry R. Bose | Zendy; William J. Mandy | Zendy; D. S. Hoare | Zendy

Open Access

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

Author(s) -

R. N. Patel,

Henry R. Bose,

William J. Mandy,

D. S. Hoare

Publication year - 1972

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.110.2.570-577.1972

Subject(s) - biochemistry , enzyme , pseudomonas , biology , methanol , alcohol oxidoreductase , alcohol dehydrogenase , ammonium , formate , alcohol , bacteria , oxidizing agent , strain (injury) , microbiology and biotechnology , chemistry , organic chemistry , catalysis , nad+ kinase , genetics , anatomy

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.

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