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 M(r) 37 000, which was converted into the enzyme subunit of M(r) 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.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology