Porcelli M, Della Ragione F, Cacciapuoti G, Cartenì-Farina M
Boll Soc Ital Biol Sper. 1980 Feb 15;56(3):245-9.
The present paper reports the study on a lyase in rat liver which decomposes S-adenosylmethionine into 5'-methylthioadenosine and alpha-amino-gamma-butyrolactone. The partial purification of this enzyme and some of its properties are discussed. S-adenosyl(5')-3-methylthiopropylamine, the decarboxylated analog of AdoMet, exerts a non-competitive inhibition of the enzyme whereas is inactive as substrate. The reported results demonstrate the relevance of the carboxyl group of AdoMet for the mechanism of the enzymatic hydrolysis of the sulfonium compound.
本文报道了对大鼠肝脏中一种裂解酶的研究，该酶可将S-腺苷甲硫氨酸分解为5'-甲硫基腺苷和α-氨基-γ-丁内酯。讨论了该酶的部分纯化及其一些性质。S-腺苷（5'）-3-甲硫基丙胺，即AdoMet的脱羧类似物，对该酶发挥非竞争性抑制作用，而作为底物则无活性。报道的结果证明了AdoMet的羧基对于锍化合物酶促水解机制的相关性。
