Abstract
The activity of catalase (EC 1.11.1.6) in E. coli was profoundly repressed by growth with such substrates as glucose, mannose, galactose, ribose, glycerol and pyruvate. The low catalase activity of the cells grown with glucose increased about twice when the cells were incubated with phosphate buffer containing yeast extract for 2 h. This increase of catalase activity was enhanced by continuous addition of H2O2 during the incubation. The increase of catalase activity was completely inhibited by chloramphenicol and puromycin. The synthesis of catalase induced by H2O2 was repressed by glucose and the repression was not eliminated by cyclic AMP.