Related Experiment Video
Updated: Aug 29, 2026

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
Published on: March 13, 2014
Chalcone isomerase family and fold: no longer unique to plants
Michael Gensheimer1, Arcady Mushegian
1Stowers Institute for Medical Research, 1000 E. 50th Street, Kansas City, MO 64110, USA. arm@stowers-institute.org
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.
Related Concept Videos
Cell Signaling in Plants
The Anatomy of Chloroplasts
Structure of Chloroplasts
A...
Asexual Reproduction
Chirality
Chiral objects exhibit a sense of handedness when they interact with another chiral object. For example, our left foot can only fit in the left shoe and not in the right shoe. Achiral objects — objects that have...
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...

