Exploitation of binding energy for catalysis and design

Summer B. Thyme (), Jordan Jarjour, Ryo Takeuchi, James J. Havranek, Justin Ashworth, Andrew M. Scharenberg, Barry L. Stoddard and David Baker ()
Additional contact information
Summer B. Thyme: Department of Biochemistry,
Jordan Jarjour: Department of Immunology,
Ryo Takeuchi: Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue, Seattle, Washington 98109, USA
James J. Havranek: Campus Box 8232, Washington University School of Medicine, 4566 Scott Avenue, St Louis, Missouri 63110, USA
Justin Ashworth: Department of Biochemistry,
Andrew M. Scharenberg: Department of Immunology,
Barry L. Stoddard: Graduate Program in Biomolecular Structure and Design,
David Baker: Department of Biochemistry,

Nature, 2009, vol. 461, issue 7268, 1300-1304

Abstract: Enzyme catalysis: asymmetry in endonucleases Enzymes use substrate-binding energy to promote ground-state association and to selectively lower the energy of the reaction transition state. Thyme et al. have determined that for the monomeric homing endonuclease I-AniI, which cleaves double-stranded DNA with high sequence specificity, mutation in the N-terminal domain of the enzyme is responsible for increasing certain kinetic parameters (KD and KM), whereas mutation in the C-terminal domain decreases another kinetic parameter (kcat). This unexpected asymmetry in the utilization of enzyme–substrate binding energy for catalysis may enable researchers to more effectively re-engineer endonucleases to cleave genomic target sites for gene therapy and other biomedical applications.

Date: 2009
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DOI: 10.1038/nature08508

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