Abstract
1. 1. Crude extracts from cells of several species of Streptomyces grown on different sources of carbon and energy, showed a constitutive ATP-dependent phosphorylating activity on glucose. Specifically inducible kinase activities for mannose and fructose were found in cells grown on each of these sugars. 2. 2. The activity on glucose corresponded to a typical bacterial glucokinase (ATP: d-glucose 6-phosphotransferase, EC 2.7.1.2). The activities on mannose and fructose corresponded to two enzymes of a novel pattern. 3. 3. The activity on mannose was due to a mannokinase (ATP:hexose 6-phosphotransferase, EC 2.7.1.7), which has been purified about 100-fold from extracts of Streptomyces violaceoruber. The K m of this enzyme for mannose was 0.05 mM. Glucose was also phosphorylated by this enzyme although with low affinity ( K m = 4 mM ). Fructose was neither a substrate nor an inhibitor. 4. 4. The inducible activity on fructose corresponded to a highly specific fructokinase (ATP: d-fructose 6-phosphotransferase, EC 2.7.1.4), which is described in the accompanying report.
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