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3ZPH

Bacterial chalcone isomerase in closed conformation from Eubacterium ramulus at 2.8 A resolution

3ZPH の概要
エントリーDOI10.2210/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
Thomsen, M.,Palm, G.J.,Hinrichs, W. (登録日: 2013-02-27, 公開日: 2014-01-15, 最終更新日: 2023-12-20)
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: 24459060
DOI: 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)
構造検証レポート
Validation report summary of 3zph
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-11に公開中

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