Oxidation of putrescine and cadaverine derivatives by diamine oxidases

Article abstract of DOI:10.1016/S0040-4020(01)90506-X

A range of putrescine and cadaverine derivatives has been synthesized and assayed as substrates for the diamine oxidases from pea seedlings and pig kidney. K_M and V_max data are reported, mainly for the pea enzyme. N-Alkylputrescines and C-alkylcadaverines are generally poorer substrates than the parent compounds with up to 4500-fold reduction in V_max. There is significantly less variation in K_M values, indicating that the binding site of the pea enzyme is relatively non-specific and that enzymic specificity lies at the catalytic stage. This suggests that poor substrates might act as convenient, short-lived inhibitors of diamine oxidases.