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. 1969 Apr;98(1):87–95. doi: 10.1128/jb.98.1.87-95.1969

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

S Sridhara a, T T Wu a,1, T M Chused a,2, E C C Lin a
PMCID: PMC249908  PMID: 4306747

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 Vmax and the apparent Km for a given substrate vary with the particular metal used.

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Selected References

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