Gensheimer Michael, Mushegian Arcady
Stowers Institute for Medical Research, 1000 E. 50th Street, Kansas City, MO 64110, USA.
Protein Sci. 2004 Feb;13(2):540-4. doi: 10.1110/ps.03395404. Epub 2004 Jan 10.
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.
查尔酮异构酶是植物异黄酮途径中的一种酶,催化查尔酮环化生成(2S)-柚皮素。查尔酮异构酶序列家族和三维折叠似乎是植物所特有的,并已被提议作为植物特异性基因标记。通过使用敏感的序列比较和折叠识别方法,我们在所有已完全测序的真菌、黏菌和许多γ-变形菌中鉴定出了与查尔酮异构酶同源的基因。直接参与该酶催化功能的残基在物种间是保守性最好的,这表明新发现的同源物具有酶活性。同时,具有查尔酮异构酶样基因的真菌和细菌物种往往缺乏上游酶查尔酮合酶的直系同源物,这表明这些物种中该途径存在新的变异。