Properties of an NAD(H)-containing methanol dehydrogenase and its activator protein from Bacillus methanolicus.

@article{Arfman1997PropertiesOA,
  title={Properties of an NAD(H)-containing methanol dehydrogenase and its activator protein from Bacillus methanolicus.},
  author={Nico Arfman and Harm J. Hektor and Leonid V. Bystrykh and Natalia I. Govorukhina and Lubbert Dijkhuizen and Joachim Frank},
  journal={European journal of biochemistry},
  year={1997},
  volume={244 2},
  pages={
          426-33
        }
}
Oxidation of C1-C4 primary alcohols in thermotolerant Bacillus methanolicus strains is catalyzed by an NAD-dependent methanol dehydrogenase (MDH), composed of ten identical 43,000-Mr subunits. Each MDH subunit contains a tightly, but non-covalently, bound NAD(H) molecule, in addition to 1 Zn2+ and 1-2 Mg2+ ions. The NAD(H) cofactor is oxidized and reduced by formaldehyde and methanol, respectively, while it remains bound to the enzyme. Incubation of MDH with methanol and exogenous NAD (coenzyme… CONTINUE READING
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