suppression of approximately 83 % of the intrinsic isotope effects in the overall reaction rate ( e.g. , kh/kd = 10 down to dv = 2.5 ) corroborates earlier kinetic data on p-hydroxybenzoate hydroxylase [ husain , m. , & massey . v. ( 1979 ) j. biol . chem . 254 , 6657 ] and suggests that these bacterial phenolic monooxygenases balance out internal transition states such that no single barrier is fully rate limiting .
C0000500
p-hydroxybenzoate hydroxylase
C0020364
monooxygenases