Kameji T, Pegg A E
Biochem J. 1987 Apr 1;243(1):285-8. doi: 10.1042/bj2430285.
The synthesis of S-adenosylmethionine (AdoMet) decarboxylase was studied by translating the rat prostate mRNA for this enzyme in a reticulocyte lysate. The protein was formed as a precursor of Mr 37,000, which was converted into the enzyme subunit of Mr 32,000 in the lysates. The presence of putrescine had no effect on the synthesis of the precursor of AdoMet decarboxylase, but accelerated its conversion into the enzyme subunit. Spermidine, spermine, decarboxylated AdoMet, AdoMet and methylglyoxal bis(guanylhydrazone) were not able to substitute for putrescine in this effect. These results indicate that, in addition to its direct activation of mammalian AdoMet decarboxylase, putrescine could increase the amount of the enzyme by increasing its production.
通过在网织红细胞裂解物中翻译大鼠前列腺中该酶的信使核糖核酸(mRNA),对S-腺苷甲硫氨酸(AdoMet)脱羧酶的合成进行了研究。该蛋白质最初以37,000道尔顿的前体形式形成,在裂解物中转化为32,000道尔顿的酶亚基。腐胺的存在对AdoMet脱羧酶前体的合成没有影响,但加速了其向酶亚基的转化。亚精胺、精胺、脱羧AdoMet、AdoMet和甲基乙二醛双(胍腙)在这种作用中不能替代腐胺。这些结果表明,除了直接激活哺乳动物AdoMet脱羧酶外,腐胺还可以通过增加其产量来增加该酶的量。