The activation of glycerol dehydrogenase from Aerobacter aerogenes by monovalent cations.

It has previously been reported that a capsulated strain of Aerobacter aerogenes, 1033, can utilize glycerol as sole source of carbon and of energy (l), and that glycerol induces this organism to form a diphosphopyridine nucleotide-linked glycerol dehydrogenase (2). This enzyme may be identical with the glycerol dehydrogenase discovered by Burton and Kaplan (3) in another strain of A. aerogenes, whose partial purification was described by Burton (4). The enzyme resembles also a glycerol dehydrogenase of Escherichiu coli described by Asnis and Brodie (5). Preliminary observations had shown that the level of glycerol dehydrogenase activity in A. czerogenes strain 1033 fluctuated greatly during different phases of growth. It seemed important to purify and characterize the enzyme before undertaking an investigation into the causes of this fluctuation. This preliminary study, described in the present paper, revealed among other properties of the enzyme a requirement for certain cations.