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• W2886885320 startingPage "6434" @default.
• W2886885320 abstract "The malarial pathogen Plasmodium falciparum (Pf) is a member of the Apicomplexa, which independently evolved a highly specific lactate dehydrogenase (LDH) from an ancestral malate dehydrogenase (MDH) via a five-residue insertion in a key active site loop. PfLDH is widely considered an attractive drug target because of its unique active site. The conservation of the apicomplexan loop suggests that a precise insertion sequence was required for the evolution of LDH specificity. Aside from a single critical tryptophan, W107f, the functional and structural roles of residues in the loop are currently unknown. Here we show that the loop is remarkably robust to mutation, as activity is resilient to radical perturbations of both loop identity and length. Thus, alternative insertions could have evolved LDH specificity as long as they contained a tryptophan in the proper location. PfLDH likely has great potential to develop resistance to drugs designed to target its distinctive active site loop." @default.
• W2886885320 created "2018-08-22" @default.
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• W2886885320 date "2018-10-25" @default.
• W2886885320 modified "2023-10-15" @default.
• W2886885320 title "Functional and Structural Resilience of the Active Site Loop in the Evolution of <i>Plasmodium</i> Lactate Dehydrogenase" @default.
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• W2886885320 doi "https://doi.org/10.1021/acs.biochem.8b00913" @default.
• W2886885320 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6247789" @default.
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• W2886885320 hasPublicationYear "2018" @default.
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