Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis

Micheline N. Ngaki, Gordon V. Louie, Ryan N. Philippe, Gerard Manning, Florence Pojer, Marianne E. Bowman, Ling Li, Elise Larsen, Eve Syrkin Wurtele () and Joseph P. Noel ()
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Micheline N. Ngaki: Development, and Cell Biology, Iowa State University
Gordon V. Louie: Howard Hughes Medical Institute, Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies
Ryan N. Philippe: Howard Hughes Medical Institute, Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies
Gerard Manning: Razavi Newman Center for Bioinformatics, The Salk Institute for Biological Studies
Florence Pojer: Howard Hughes Medical Institute, Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies
Marianne E. Bowman: Howard Hughes Medical Institute, Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies
Ling Li: Development, and Cell Biology, Iowa State University
Elise Larsen: Howard Hughes Medical Institute, Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies
Eve Syrkin Wurtele: Development, and Cell Biology, Iowa State University
Joseph P. Noel: Howard Hughes Medical Institute, Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies

Nature, 2012, vol. 485, issue 7399, 530-533

Abstract: The diffusion limited stereospecific enzyme chalcone isomerase represents the adaptive evolution of a catalytically perfected enzyme from non-catalytic, fatty-acid-binding proteins (FAPs) with contemporary roles in plant fatty-acid metabolism as evidenced by altered fatty acid content and marked reproductive defects in Arabidopsis thaliana plants bearing FAP knockouts.

Date: 2012
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DOI: 10.1038/nature11009

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