Conformational control of ovoperoxidase catalysis in the sea urchin fertilization membrane.
The ovoperoxidase-catalyzed oxidation of iodide has been investigated as a function of pH for the homogeneous enzyme and for ovoperoxidase incorporated into several forms of the egg fertilization membrane. The pH dependent hysteresis previously observed in purified ovoperoxidase (Deits, T. L., Shapiro, B. M. (1985) J. Biol. Chem. 260, 7882-7888) is entirely absent in ovoperoxidase incorporated into the mature fertilization membrane, where the enzyme is bound noncovalently in vivo. The pH activity profile of ovoperoxidase incorporated into the mature fertilization membrane closely resembles the profile observed only transiently in purified ovoperoxidase subjected to a rapid downward pH shift. These observations can be accounted for by our previously presented mechanism for ovoperoxidase hysteresis (ibid.). We hypothesize that ovoperoxidase, upon incorporation into the fertilization membrane, is restricted to a limited subset of the conformational states available to the purified enzyme. This matrix-dependent conformational restriction is a novel control mechanism that serves to enhance the catalytic activity of ovoperoxidase upon its assembly into the fertilization membrane and thereby modulates ovoperoxidase catalysis in the vicinity of the developing egg.
D000818:Animals; D005089:Exocytosis; D006863:Hydrogen-Ion Concentration; D007454:Iodides / Q000378:metabolism; D010544:Peroxidases / Q000378:metabolism*; D011487:Protein Conformation; D012617:Sea Urchins; D013320:Strongyloidea; D014817:Vitelline Membrane / Q000201:enzymology*
D007454:Iodides; D010544:Peroxidases