Ferrous-activated nicotinamide adenine dinucleotide-linked dehydrogenase from a mutant of Escherichia coli capable of growth on 1, 2-propanediol.
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.
D002499:Centrifugation, Density Gradient; D002845:Chromatography; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D000431:Ethanol / Q000378:metabolism; D005990:Glycerol / Q000378:metabolism; D006018:Glycols / Q000378:metabolism; D007501:Iron / Q000494:pharmacology*; D007700:Kinetics; D008345:Manganese / Q000494:pharmacology; D009154:Mutation; D009243:NAD; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D011409:Propylene Glycols / Q000378:metabolism*; D013053:Spectrophotometry
D006018:Glycols; D011409:Propylene Glycols; D009243:NAD; D000431:Ethanol; D008345:Manganese; D007501:Iron; D010088:Oxidoreductases; D005990:Glycerol