title: Completing the folate biosynthesis pathway in Plasmodium falciparum: p-aminobenzoate is produced by a highly divergent promiscuous aminodeoxychorismate lyase.
abstract: Enzymes that produce or recycle folates are the targets of widely used antimalarial drugs. Despite the interest in the folate metabolism of Plasmodium falciparum, the molecular identification of ADCL (aminodeoxychorismate lyase), which synthesizes the p-aminobenzoate moiety of folate, remained unresolved. In the present study, we demonstrate that the plasmodial gene PF14_0557 encodes a functional ADCL and report a characterization of the recombinant enzyme.
authors: *Department of Life Sciences, Laboratory of Biochemistry, Molecular Biology and Bioinformatics, University of Parma, 43124 Parma, Italy.
authors: Giovanni
authors: G
authors: Magnani
authors: Michela
authors: M
authors: Lomazzi
authors: Alessio
authors: A
authors: Peracchi
mesh_terms: D000818:Animals; D019295:Computational Biology; D005492:Folic Acid / Q000096:biosynthesis*; D007652:Oxo-Acid-Lyases / Q000235:genetics* / Q000378:metabolism*; D010963:Plasmodium falciparum / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism*; D015800:Protozoan Proteins / Q000235:genetics* / Q000378:metabolism; D011817:Rabbits; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D062366:para-Aminobenzoates / Q000378:metabolism*
chemical_list: D015800:Protozoan Proteins; D011994:Recombinant Proteins; D062366:para-Aminobenzoates; D005492:Folic Acid; D007652:Oxo-Acid-Lyases; C066600:aminodeoxychorismate lyase