Stimulation of the microsomal alkylglycerol monooxygenase by catalase.
Liver cytosol contains a heat-sensitive nondialyzable soluble factor necessary for maximal activity of the alkylglycerol monooxygenase present in rat liver microsomes. In this report, we demonstrate that the stimulatory component in rat liver supernatant is catalase. Catalase functions to protect the enzyme from inactivation by H2O2 in addition to its documented ability to retard the noenzymatic oxidation of the pterin cofactor. The protective effect of catalase on alkylglycerol monooxygenase and on the aromatic amino acid hydroxylase systems indicates that H2O2 sensitivity is a general feature of pterin-dependent hydroxylases.
D000818:Animals; D002374:Catalase / Q000378:metabolism*; D003600:Cytosol / Q000201:enzymology; D004789:Enzyme Activation; D005989:Glycerides; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008862:Microsomes, Liver / Q000187:drug effects / Q000201:enzymology*; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D051381:Rats; D013997:Time Factors
D005989:Glycerides; D006861:Hydrogen Peroxide; D006899:Mixed Function Oxygenases; D002374:Catalase