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The anaerobicl -α-glycerophosphate (l -α-GP) dehydrogenase ofEscherichia coli was purified approximately 40-fold. The activity of the dehydrogenase, although not affected by the addition of pyridine nucleotides, was stimulated three- to fourfold by flavine adenine dinucleotide (K m about 10−7 m ) and up to 10-fold by flavine mononucleotide (K m about 10−4 m ). Maximal activity of the enzyme was found only in the combined presence of saturating concentrations of both flavines (stimulation by a factor of 10 to 15). The dependence of the rate of the reaction on the concentration ofl -α-GP was complex in the presence of both flavines, but in the presence of flavine adenine dinucleotide alone the kinetics were of the Michaelis-Menten type with theK m forl -α-GP being about 10−4 m . The product of the reaction was identified as dihydroxyacetone phosphate, and the molecular weight of the dehydrogenase was estimated to be 80,000 ± 10,000. Phenazine methosulfate, menadione and ferricyanide served as artificial acceptors for the dehydrogenase. The enzyme was sensitive to iodoacetate,p -chloromercuribenzoate, andN -ethymaleimide.

Purification and Properties of the Flavine-Stimulated Anaerobicl-α-Glycerophosphate Dehydrogenase ofEscherichia coli