抄録
With the use of crystalline preparations of tyramine oxidase of Sarcina lutea, substrate and inhibitor specificities of the enzyme were investigated. The enzyme oxidized tyramine and dopamine at almost the same rates. Other monoamines, diamines, polyamines and amino acids were not oxidized at all. The oxidation of tyramine proceeded as follows: Tyramine+O2+H2O→p-Hydroxyphenylacetaldehyde+NH3+H2O2. Ammonia and hydrogen peroxide were formed in stoichiometric amounts.
The enzyme was not inhibited by carbonyl reagents, such as hydroxylamine, hydrazine, semicarbazide and isoniazid, but was inhibited by p-CMB and iproniazid.