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Design of protein catalysts.
Journal article

Design of protein catalysts.

  • Hilvert D Laboratory of Organic Chemistry, ETH Zürich, 8093 Zürich, Switzerland. hilvert@org.chem.ethz.ch
  • 2013-06-11
Published in:
  • Annual review of biochemistry. - 2013
Catalysis
Catalytic Domain
Computational Biology
Directed Molecular Evolution
Enzymes
Models, Molecular
Protein Engineering
Proteins
English Diverse engineering strategies have been developed to create enzymes with novel catalytic activities. Among these, computational approaches hold particular promise. Enzymes have been computationally designed to promote several nonbiological reactions, including a Diels-Alder cycloaddition, proton transfer, multistep retroaldol transformations, and metal-dependent hydrolysis of phosphotriesters. Although their efficiencies (kcat/KM = 0.1-100 M(-1) s(-1)) are typically low compared with those of the best natural enzymes (10(6)-10(8) M(-1) s(-1)), these catalysts are excellent starting points for laboratory evolution. This review surveys recent progress in combining computational and evolutionary approaches to enzyme design, together with insights into enzyme function gained from studies of the engineered catalysts.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/76126
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