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Photo Lynn Kamerlin

Lynn Kamerlin

Professor

Photo Lynn Kamerlin

Cooperativity and flexibility in enzyme evolution

Author

  • Anna Pabis
  • Valeria A Risso
  • Jose M Sanchez-Ruiz
  • Shina Cl Kamerlin

Summary, in English

Enzymes are flexible catalysts, and there has been substantial discussion about the extent to which this flexibility contributes to their catalytic efficiency. What has been significantly less discussed is the extent to which this flexibility contributes to their evolvability. Despite this, recent years have seen an increasing number of both experimental and computational studies that demonstrate that cooperativity and flexibility play significant roles in enzyme innovation. This review covers key developments in the field that emphasize the importance of enzyme dynamics not just to the evolution of new enzyme function(s), but also as a property that can be harnessed in the design of new artificial enzymes.

Publishing year

2018-02

Language

English

Pages

83-92

Publication/Series

Current Opinion in Structural Biology

Volume

48

Document type

Journal article review

Publisher

Elsevier

Keywords

  • Amino Acid Motifs
  • Animals
  • Aryldialkylphosphatase/chemistry
  • Bacteria/classification
  • Biocatalysis
  • Catalytic Domain
  • Evolution, Molecular
  • Humans
  • Models, Molecular
  • Phosphoric Monoester Hydrolases/chemistry
  • Phylogeny
  • Protein Conformation
  • Structure-Activity Relationship
  • Substrate Specificity
  • Tetrahydrofolate Dehydrogenase/chemistry
  • beta-Lactamases/chemistry

Status

Published

ISBN/ISSN/Other

  • ISSN: 1879-033X