Enzyme promiscuity: evolutionary and mechanistic aspects.

By O. Khersonsky, C. Roodveldt, Dan S. Tawfik. Current Opinion in Chemical Biology, 2006

620 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/1c2b0928db92ebabe79db097244a6af55b1ce5ff

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Citations in the corpus

Highly active and selective endopeptidases with programmed substrate specificities. (2008, background): “The enzyme variants isolated here do not exhibit the relaxed specificity or low activity of primeval “generalist” enzymes that are typically obtained by standard laboratory-directed evolution 11 , 26 .”
Enzyme promiscuity: a mechanistic and evolutionary perspective. (2010, background): “More recent reviews focused on practical implications of promiscuity (1, 10–12), on promiscuity and divergence mechanistic aspects of promiscuity (1, 17), and on promiscuity in the context of protein evolution and design (17, 18).”
Probing the Mutational Interplay between Primary and Promiscuous Protein Functions: A Computational-Experimental Approach (2012, background): “Furthermore, as briefly elaborated below, promiscuity likely plays an essential role in the development of new functions through divergent evolution [3,5,8,16–20].”
A structural model of latent evolutionary potentials underlying neutral networks in proteins (2007, background): “As far as protein function is concerned, enzymes have long been known to be promiscuous (James and Tawfik, 2001; Khersonsky et al., 2006).”
Adaptive laboratory evolution – principles and applications for biotechnology (2013, neutral): “evolution of novel functions [144].”
A de novo protein binding pair by computational design and directed evolution (2011, background): “The Orientational Specificity of Protein Complexes In vitro evolved proteins are frequently found to be promiscuous, exhibiting a wide range of crossreactivity (Aharoni et al., 2005; Bridgham et al., 2006; Collins et al., 2006; James and Tawfik, 2003; Khersonsky et al., 2006).”
Evolutionary Conserved Positions Define Protein Conformational Diversity (2016, background): “Enzyme catalysis[16], signal transduction[17], protein recognition specificity [18], promiscuity[19], allosterism[20,21], origin of new protein functional adaptation and evolution[15,22,23] can be counted among others.”
Latent evolutionary potentials under the neutral mutational drift of an enzyme (2007, background): “Previous works also demonstrated that these promiscuous activities could amply evolve (30–200-fold, in response to 1–4 mutations), typically at the expense of large decreases in other promiscuous functions (100–1000-fold), yet with much smaller effects (0–22-fold decreases) on the native lactonase f”