title: Extremely rapid turnover of S-adenosylmethionine decarboxylase in Crithidia fasciculata.
abstract: 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.
authors.affiliation: Department of Physiological Sciences, Lund University, Sweden.
authors.forename: Sima
authors.initials: S
authors.lastname: Nasizadeh
authors.forename: Lo
authors.initials: L
authors.lastname: Persson
mesh_terms: D012437:Adenosylmethionine Decarboxylase / Q000378:metabolism*; D000818:Animals; D002455:Cell Division; D016831:Crithidia fasciculata / Q000201:enzymology* / Q000254:growth & development; D003513:Cycloheximide / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D006207:Half-Life; D007700:Kinetics; D011073:Polyamines / Q000494:pharmacology; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity
chemical_list: D011073:Polyamines; D011500:Protein Synthesis Inhibitors; D003513:Cycloheximide; D012437:Adenosylmethionine Decarboxylase