Studies on the possible mechanism of inactivation of phenylalanine hydroxylase by destructive oxygen species.
The enzymic hydroxylation of phenylalanine by phenylalanine hydroxylase (E.C. 1.14.16.1.) in vitro is dependent on the presence of hydrogen peroxide removing processes. The loss of phenylalanine hydroxylase activity can be prevented to the same extent by catalase as well as the presence of optimized amounts of both peroxidase and superoxide dismutase. Peroxidase alone exhibited only two third of the maximal protective effect of catalase whereas superoxide dismutase alone was not able to exert any protective influence on phenylalanine hydroxylase. These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H2O2 and the tetrahydropterin cofactor.
D000818:Animals; D002374:Catalase / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D010544:Peroxidases / Q000378:metabolism; D010651:Phenylalanine Hydroxylase / Q000037:antagonists & inhibitors*; D051381:Rats; D013053:Spectrophotometry / Q000379:methods; D013482:Superoxide Dismutase / Q000378:metabolism
D010544:Peroxidases; D002374:Catalase; D010651:Phenylalanine Hydroxylase; D013482:Superoxide Dismutase