Functions of tryptophan residues in EWGWS insert of Plasmodium falciparum enolase.

ABSTRACT: Plasmodium falciparum enolase (Pfeno) is a dimeric enzyme with multiple moonlighting functions. This enzyme is thus a potential target for anti-malarial treatments. A unique feature of Pfeno is the presence of a pentapeptide insert ¹⁰⁴ EWGWS ¹⁰⁸. The functional role of tryptophan residues in this insert was investigated using site-directed mutagenesis. Replacement of these two Trp residues with alanines (or lysines) resulted in a near complete loss of enolase activity and dissociation of the normal dimeric form into monomers. Molecular modeling indicated that ³⁴⁰R forms π-cation bonds with the aromatic rings of ¹⁰⁵W and ⁴⁶Y. Mutation induced changes in the interactions among these three residues were presumably relayed to the in

SUBMITTER: Dutta S 

PROVIDER: S-EPMC5494301 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature