Evolutionary strategy for optimization of GSH binding and catalysis in Alpha, Pi, Mu and theta glutathione transferases

Anna Maria Caccuri, Giovanni Antonini, Philip G. Board, Jack Flanagan, Michael W. Parker, Roberto Paolesse, Paola Turella, Giorgio Federici, Mario Lo Bello, Giorgio Ricci*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)

    Abstract

    The substrate binding mechanism and catalysis of the human glutathione transferase T2-2 have been studied and compared to those found in the more recently evolved Alpha, Mu and Pi class isoenzymes. The evolution strategy for the optimization of the binding process is based on the shift from a single-step to a multi-step interaction with the substrate. An evolutionary pressure in terms of flexibility of the protein and of proper orientation of the substrate may also explain the relevant differences of the catalytic properties found among the 'old' and 'young' isoenzymes.

    Original languageEnglish
    Pages (from-to)163-166
    Number of pages4
    JournalChemico-Biological Interactions
    Volume133
    Issue number1-3
    Publication statusPublished - 28 Feb 2001

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