Trypanosoma brucei S-adenosylmethionine decarboxylase N terminus is essential for allosteric activation by the regulatory subunit prozyme

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Abstract

Background: Trypanosoma brucei S-adenosylmethionine decarboxylase (AdoMetDC) is activated by heterodimerization with a catalytically dead paralog, prozyme. Results: Trypanosomatid-specific residues in the AdoMetDC N terminus are essential for prozyme-mediated activation but not for heterodimerization. Conclusion: AdoMetDC activation likely involves a conformational change of the N-terminal peptide. Significance: Development of conformationally sensitive AdoMetDC inhibitors may provide a species-selective mechanism to inhibit trypanosomatid AdoMetDCs.

Original languageEnglish (US)
Pages (from-to)5232-5240
Number of pages9
JournalJournal of Biological Chemistry
Volume288
Issue number7
DOIs
StatePublished - Feb 15 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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