Changing the substrate specificity of cytochrome c peroxidase using directed evolution
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A review with 15 refs. Directed mol. evolution of enzymes and proteins has emerged as an extremely powerful method to create proteins with novel properties, both for practical applications as well as for mechanistic studies. To demonstrate the underlying p ...
Cytochrome c peroxidase (CCP) from Saccharomyces cerevisiae was subjected to directed mol. evolution to generate mutants with increased activity against the classical peroxidase substrate, guaiacol, thus changing the substrate specificity of CCP from the p ...
An extensive random mutagenesis study on the function of nine residues in the subunit binding site of FimC was conducted to evaluate the mol. mechanisms of subunit binding by FimC and the contribution of chaperone surface residues. Five plasmid libraries o ...
Deutsche Akademie der Naturforscher Leopoldina2001
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