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Extremely rapid turnover of S‐adenosylmethionine decarboxylase in Crithidia fasciculata
Author(s) -
Nasizadeh Sima,
Persson Lo
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00986-4
Subject(s) - crithidia fasciculata , adenosylmethionine decarboxylase , biochemistry , enzyme , chemistry , enzyme assay , specific activity , biology , ornithine decarboxylase
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.