3ZPH
Bacterial chalcone isomerase in closed conformation from Eubacterium ramulus at 2.8 A resolution
3ZPH の概要
エントリーDOI | 10.2210/pdb3zph/pdb |
分子名称 | CHALCONE ISOMERASE, GLYCEROL, CHLORIDE ION, ... (4 entities in total) |
機能のキーワード | isomerase, flavonoid degradation |
由来する生物種 | EUBACTERIUM RAMULUS |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 195042.70 |
構造登録者 | |
主引用文献 | Gall, M.,Thomsen, M.,Peters, C.,Pavlidis, I.V.,Jonczyk, P.,Grunert, P.P.,Beutel, S.,Scheper, T.,Gross, E.,Backes, M.,Geissler, T.,Ley, J.P.,Hilmer, J.M.,Krammer, G.,Palm, G.J.,Hinrichs, W.,Bornscheuer, U.T. Enzymatic conversion of flavonoids using bacterial chalcone isomerase and enoate reductase. Angew.Chem.Int.Ed.Engl., 53:1439-1442, 2014 Cited by PubMed Abstract: Flavonoids are a large group of plant secondary metabolites with a variety of biological properties and are therefore of interest to many scientists, as they can lead to industrially interesting intermediates. The anaerobic gut bacterium Eubacterium ramulus can catabolize flavonoids, but until now, the pathway has not been experimentally confirmed. In the present work, a chalcone isomerase (CHI) and an enoate reductase (ERED) could be identified through whole genome sequencing and gene motif search. These two enzymes were successfully cloned and expressed in Escherichia coli in their active form, even under aerobic conditions. The catabolic pathway of E. ramulus was confirmed by biotransformations of flavanones into dihydrochalcones. The engineered E. coli strain that expresses both enzymes was used for the conversion of several flavanones, underlining the applicability of this biocatalytic cascade reaction. PubMed: 24459060DOI: 10.1002/anie.201306952 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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