ABSTRACT
This chapter explores amine oxidases whose products are essential components of another system. The major part of this contribution, however, will be devoted to a discussion of the biological function of amine oxidases. It took a long time to reach a safe identification of nonproteinaceous components of amine oxidases. The enzymology of polyamine oxidation began with some simple observations pertaining to the degradation of spermine and spermidine by diamine oxidase. In 1951, for the first time, the oxidative deamination of monoamine, diamines, and polyamines was reviewed together. Aminoaldehydes formed from polyamines interact with DNA and are toxic to virus, bacteria, parasites, and tumor cells. Growth and differentiation processes are closely related to cellular polyamine levels; hence the vital processes may be regulated by modulating cellular amine levels". U. Bachrach proposes that "amine oxidases catalyze the oxidation of amines or polyamines and thereby regulate their cellular levels.
