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. 1988 Jul;170(7):3189–3193. doi: 10.1128/jb.170.7.3189-3193.1988

Purification and properties of formate dehydrogenase from Moraxella sp. strain C-1.

Y Asano 1, T Sekigawa 1, H Inukai 1, A Nakazawa 1
PMCID: PMC211267  PMID: 3384805

Abstract

NAD+-dependent formate dehydrogenase was screened in various bacterial strains. Facultative methanol-utilizing bacteria isolated from soil samples, acclimated to a medium containing methanol and formate at pH 9.5, were classified as members of the genus Moraxella. From a crude extract of Moraxella sp. strain C-1, formate dehydrogenase was purified to homogeneity, as judged by disc gel electrophoresis. The enzyme has an isoelectric point of 3.9 and a molecular weight of approximately 98,000. The enzyme is composed of two identical subunits with molecular weights of about 48,000. The apparent Km values for sodium formate and NAD+ were calculated to be 13 mM and 0.068 mM, respectively.

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Selected References

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