| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5915635 | Molecular and Biochemical Parasitology | 2011 | 10 Pages |
Abstract
⺠Codon harmonization resulted in soluble expression of Plasmodium falciparum S-adenosylmethionine decarboxylase (AdoMetDC). ⺠PfAdoMetDC exists as both monomers and dimers in vitro. ⺠Residue Cys505 is involved in disulphide bond formation at the dimer interface. ⺠Kinetics analyses showed that PfAdoMetDC lacks an allosteric regulator. ⺠Even though structural similarity exists, PfAdoMetDC belongs to its own protein subclass, namely 2b-III.
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Authors
Marni Williams, Janina Sprenger, Esmaré Human, Salam Al-Karadaghi, Lo Persson, Abraham I. Louw, Lyn-Marie Birkholtz,