Tetramerization and Cooperativity in Plasmodium falciparum Glutathione S-Transferase Are Mediated by Atypic Loop 113–119

Glutathione S-transferase of Plasmodium falciparum (PfGST) displays a peculiar dimer to tetramer transition that causes full enzyme inactivation and loss of its ability to sequester parasitotoxic hemin. Furthermore, binding of hemin is modulated by a cooperative mechanism. Site-directed mutagenesis,...

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Hlavní autoři: Liebau, Eva, Dawood, Kutayba F., Fabrini, Raffaele, Fischer-Riepe, Lena, Perbandt, Markus, Stella, Lorenzo, Pedersen, Jens Z., Bocedi, Alessio, Petrarca, Patrizia, Federici, Giorgio, Ricci, Giorgio
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2009
Témata:
Enzyme Catalysis and Regulation
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2755937/
https://ncbi.nlm.nih.gov/pubmed/19531494
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.015198
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