4E14

Crystal structure of kynurenine formamidase conjugated with phenylmethylsulfonyl fluoride

4E14 の概要

• エントリーDOI: 10.2210/pdb4e14/pdb
• 関連するPDBエントリー: 4E11 4E15
• 分子名称: kynurenine formamidase, 1,2-ETHANEDIOL, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: alpha/beta hydrolase fold, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35643.36

構造登録者

Han, Q.,Robinson, H.,Li, J. (登録日: 2012-03-05, 公開日: 2012-06-27, 最終更新日: 2023-09-13)

主引用文献

Han, Q.,Robinson, H.,Li, J.
Biochemical identification and crystal structure of kynurenine formamidase from Drosophila melanogaster.
Biochem.J., 446:253-260, 2012

PubMed Abstract: KFase (kynurenine formamidase), also known as arylformamidase and formylkynurenine formamidase, efficiently catalyses the hydrolysis of NFK (N-formyl-L-kynurenine) to kynurenine. KFase is the second enzyme in the kynurenine pathway of tryptophan metabolism. A number of intermediates formed in the kynurenine pathway are biologically active and implicated in an assortment of medical conditions, including cancer, schizophrenia and neurodegenerative diseases. Consequently, enzymes involved in the kynurenine pathway have been considered potential regulatory targets. In the present study, we report, for the first time, the biochemical characterization and crystal structures of Drosophila melanogaster KFase conjugated with an inhibitor, PMSF. The protein architecture of KFase reveals that it belongs to the α/β hydrolase fold family. The PMSF-binding information of the solved conjugated crystal structure was used to obtain a KFase and NFK complex using molecular docking. The complex is useful for understanding the catalytic mechanism of KFase. The present study provides a molecular basis for future efforts in maintaining or regulating kynurenine metabolism through the molecular and biochemical regulation of KFase.

PubMed: 22690733
DOI: 10.1042/BJ20120416

実験手法

X-RAY DIFFRACTION (1.64 Å)