Directed Evolution of Protein Catalysts.

By C. Zeymer, Donald Hilvert. Annual Review of Biochemistry, 2018

370 citations recorded by the source corpus.

Directed evolution is a powerful technique for generating tailor-made enzymes for a wide range of biocatalytic applications. Following the principles of natural evolution, iterative cycles of mutagenesis and screening or selection are applied to modify protein properties, enhance catalytic activities, or develop completely new protein catalysts for non-natural chemical transformations. This review briefly surveys the experimental methods used to generate genetic diversity and screen or select for improved enzyme variants. Emphasis is placed on a key challenge, namely how to generate novel catalytic activities that expand the scope of natural reactions. Two particularly effective strategies, exploiting catalytic promiscuity and rational design, are illustrated by representative examples of successfully evolved enzymes. Opportunities for extending these approaches to more complex biocatalytic systems are also considered.

Subfields: Molecular Biology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/9ed48e1366d3636ac30f5dae3e70c05d77f29910

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Citations in the corpus

• Machine learning-assisted directed protein evolution with combinatorial libraries (2019, background): “In some cases, engineering to enhance desirable features can be accomplished reliably by directed evolution, in which beneficial mutations are identified and accumulated through an iterative process of mutation and testing of hundreds to thousands of variants in each generation (2 – 4).”