Purification and properties of 2-ketogluconokinase from Aerobacter aerogenes.

A specific kinase for the phosphorylation of 2-ketogluconate with adenosine triphosphate has been found in Pseudomonas JEuorescens grown on glucose (l), in Aerobacter cloacae grown on 2-ketogluconate (2), and in a number of other bacterial species. In P. jluorescens, phosphorylation of 2-ketogluconate is a major step in the sequence of glucose catabolism (3) and hence is induced by growth on glucose, whereas in A. cloacae (2) and Leuconostoc mesenteroides (4), 2-ketogluconate is not an intermediate in glucose dissimilation. Thus, the kinase is induced only during growth on 2-ketogluconate. It has been shown with all of these organisms, however, that 2-ketogluconokinase is distinct from gluconokinase. Although 2-ketogluconokinase has been purified from P. Jluorescens grown on glucose, consistently higher activity has been found in Aerobacter aerogenes grown on 2-ketogluconate. This paper describes the purification and properties of the kinase from that source as well as an improved method for synthesis and isolation of 2-keto-6-phosphogluconate.