Ferrous-activated Nicotinamide Adenine Dinucleotide-linked Dehydrogenase from a Mutant of Escherichia coli Capable of Growth on 1,2-Propanediol

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Abstract
A nicotinamide adenine dinucleotide-linked dehydrogenase has been partially purified from a mutant of Escherichia coli K-12 able to grow on l -1,2-propanediol as carbon and energy source. This enzyme catalyzes the dehydrogenation at carbon 1 of l -1,2-propanediol, glycerol, 1,3-propanediol, ethylene glycol, and ethyl alcohol. The purified protein requires added ferrous or managanous ions. The V max and the apparent K m for a given substrate vary with the particular metal used.