Monoamine Oxidase

Literature References: Since its first description by Hare in 1928 as an enzyme which catalyzed the oxidative deamination of tyramine, it has been found to be widely distributed in animals. This enzyme, which catalyzes the oxidative deamination of a variety of biogenic amines, such as serotonin, norepinephrine, epinephrine, tyramine and dopamine, deaminates compounds in which the amine group is attached to the terminal carbon group. Enzymes other than the classical amine oxidase which catalyze the oxidative deamination of amines, have been found in animals, plants and bacteria. In contrast to the classical amine oxidase, they are inhibited by carbonyl reagents and do not act on N-substituted amines. Enzymes of this group include: oxidases in microorganisms, spermine oxidase, mescaline oxidase (of rabbit liver), plant amine oxidase, and histaminase, q.v. Structural studies: Achee, Biochemistry 7, 4329 (1968). Multiple forms of rat brain monoamine oxidase: M. B. H. Youdim et al., Nature 223, 626 (1969). Review: H. Blaschko "Amine Oxidase" in The Enzymes vol. 8, P. D. Boyer et al., Eds. (Academic Press, New York, 2nd ed., 1963) pp 337-351. Book: Monoamine Oxidase: Structure, Function and Altered Functions, T. P. Singer et al., Eds. (Academic Press, New York, 1980) 557 pp.