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Published online before print January 10, 2004, 10.1110/ps.03395404
Protein Science (2004), 13:540-544. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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FOR THE RECORD

Chalcone isomerase family and fold: No longer unique to plants

Michael Gensheimer1 and Arcady Mushegian1,2

1 Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA
2 Department of Microbiology, Molecular Genetics, and Immunology, University of Kansas Medical Center, Kansas City, Kansas 66160, USA

(RECEIVED August 28, 2003; FINAL REVISION October 30, 2003; ACCEPTED October 30, 2003)



Abstract

Chalcone isomerase, an enzyme in the isoflavonoid pathway in plants, catalyzes the cyclization of chalcone into (2S)-naringenin. Chalcone isomerase sequence family and three-dimensional fold appeared to be unique to plants and has been proposed as a plant-specific gene marker. Using sensitive methods of sequence comparison and fold recognition, we have identified genes homologous to chalcone isomerase in all completely sequenced fungi, in slime molds, and in many gammaproteobacteria. The residues directly involved in the enzyme’s catalytic function are among the best conserved across species, indicating that the newly discovered homologs are enzymatically active. At the same time, fungal and bacterial species that have chalcone isomerase-like genes tend to lack the orthologs of the upstream enzyme chalcone synthase, suggesting a novel variation of the pathway in these species.

Keywords: Isoflavonoid pathway; chalcone isomerase; comparative sequence analysis

Reprint requests to: Arcady Mushegian, Stowers Institute for Medical Research, 1000 E. 50th Street, Kansas City, MO 64110, USA; e-mail: arm{at}stowers-institute.org; fax: (816) 926-2041.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03395404.


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