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.

Completing the folate biosynthesis pathway in Plasmodium falciparum: p-aminobenzoate is produced by a highly divergent promiscuous aminodeoxychorismate lyase / Magnani, Giovanni; Lomazzi, Michela; Peracchi, Alessio. - In: BIOCHEMICAL JOURNAL. - ISSN 0264-6021. - 455:(2013), pp. 149-155. [10.1042/BJ20130896]

Completing the folate biosynthesis pathway in Plasmodium falciparum: p-aminobenzoate is produced by a highly divergent promiscuous aminodeoxychorismate lyase

MAGNANI, GIOVANNI;LOMAZZI, Michela;PERACCHI, Alessio
2013-01-01

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.
2013
Completing the folate biosynthesis pathway in Plasmodium falciparum: p-aminobenzoate is produced by a highly divergent promiscuous aminodeoxychorismate lyase / Magnani, Giovanni; Lomazzi, Michela; Peracchi, Alessio. - In: BIOCHEMICAL JOURNAL. - ISSN 0264-6021. - 455:(2013), pp. 149-155. [10.1042/BJ20130896]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11381/2695282
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