| Literature DB >> 5022170 |
R N Patel, H R Bose, W J Mandy, D S Hoare.
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.Entities:
Mesh:
Substances:
Year: 1972 PMID: 5022170 PMCID: PMC247450 DOI: 10.1128/jb.110.2.570-577.1972
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490