Extremely rapid turnover of S‐adenosylmethionine decarboxylase in Crithidia fasciculata

FEBS Letters

Nasizadeh, Sima¹  Persson, Lo¹ 

[1] Department of Physiological Sciences, Lund University, BMC F-13, S-221 84 Lund, Sweden

关键词: Polyamines;    Enzyme turnover;    S-adenosylmethionine decarboxylase;    Trypanosomal;    Crithidia fasciculata;    AdoMet;    S-adenosylmethionine;    AdoMetDC;    S-adenosylmethionine decarboxylase;    ODC;    ornithine decarboxylase;    DFMO;    difluoromethylornithine;    MGBG;    methylglyoxal-bis(guanylhydrazone);    IC50;    concentration that inhibits 50% of the enzyme activity;   

DOI  :  10.1016/S0014-5793(03)00986-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The activity of S-adenosylmethionine decarboxylase (AdoMetDC) in Crithidia fasciculata was shown to be correlated to the growth of the parasite. An increase in activity was observed during exponential growth. Inhibition of protein synthesis induced an extremely rapid decay of AdoMetDC activity. The half-life of the enzyme was estimated to be about 3 min, which is the shortest half-life ever recorded for an eukaryotic AdoMetDC. The reduction in AdoMetDC activity was correlated with a decrease in AdoMetDC protein content, demonstrating a rapid turnover of the enzyme. No polyamine-mediated feedback regulation of AdoMetDC was observed in the parasite.

【 授权许可】

Unknown