Characterization of leptospiral catalase and peroxidase.
Peroxidase from Leptospira biflexa strain B-16 ad catalase from Leptospira interrogans canicola Hond Utrecht were characterized and compared and both appeared to be heme enzymes as judged by their inhibition profiles and rapid inactivation during catalysis. Neither enzyme exhibited monovalent or divalent cation requirements. Dialysis of cell-free extracts resulted in loss of peroxidase activity but catalase was unaffected by this procedure. Peroxidase had a Km for H2O2 of 12.5 microM while catalase had a Km of 70 mM for H2O2. Catalase and peroxidase were physically separated by sedimentation in linear sucrose gradients. The specific activities of each enzyme seemed to be a function of the state of growth at which the cells were harvested and both enzymes were found associated with membranes, peroxidase by hydrophobic and catalase by ionic interactions. Speculative deductions are presented concerning the phylogenetic interrelationships of both enzymes as well as their significance in the biology and pathogenicity of leptospires.
D002374:Catalase / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007919:Leptospira / Q000201:enzymology*; D007921:Leptospira interrogans / Q000201:enzymology; D010544:Peroxidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*
D010544:Peroxidases; D002374:Catalase