Computer-aided design of the stability of pyruvate formate-lyase from Escherichia coli by site-directed mutagenesis.

Abstract excerpt

Using computer-aided design of single-site mutations, three amino acid residues determined by changes in folding free energy between wild-type (wt) and mutant proteins were exchanged to enhance the stability of pyruvate formate-lyase (PFL). The mutant enzymes were tested for properties such as optimum temperature, optimum pH, kinetic parameters, and stability to temperature. There were two mutant variants,...

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