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Mutational analysis of Plasmodium falciparum dihydrofolate reductase: the role of aspartate 54 and phenylalanine 223 on catalytic activity and antifolate binding.

Molecular and biochemical parasitology - 1 May 2002

Sirawaraporn Worachart, Sirawaraporn Rachada, Yongkiettrakul Suganya, Anuwatwora Amornpol, Rastelli Guilio, Kamchonwongpaisan Sumalee, Yuthavong Yongyuth

Abstract excerpt

The catalytic activity and ability to confer resistance to antifolates of Plasmodium falciparum dihydrofolate reductase (pfDHFR) through single and double mutations at Asp-54 and Phe-223 were investigated. A single Asp54Glu (D54E) mutation in the pfDHFR domain greatly decreased the catalytic activity of the enzyme and affected both the K(m) values for the substrate dihydrofolate and the K(i) values for...

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PMID: 12034452
DOI: 10.1016/s0166-6851(02)00035-x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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