Biochemical characterisation and novel classification of monofunctional S-adenosylmethionine decarboxylase of Plasmodium falciparum

► Codon harmonization resulted in soluble expression of Plasmodium falciparum S-adenosylmethionine decarboxylase (AdoMetDC). ► PfAdoMetDC exists as both monomers and dimers in vitro. ► Residue Cys505 is involved in disulphide bond formation at the dimer interface. ► Kinetics analyses showed that PfAdoMetDC lacks an allosteric regulator. ► Even though structural similarity exists, PfAdoMetDC belongs to its own protein subclass, namely 2b-III.