4E14
Crystal structure of kynurenine formamidase conjugated with phenylmethylsulfonyl fluoride
Summary for 4E14
| Entry DOI | 10.2210/pdb4e14/pdb |
| Related | 4E11 4E15 |
| Descriptor | kynurenine formamidase, 1,2-ETHANEDIOL, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | alpha/beta hydrolase fold, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 35643.36 |
| Authors | Han, Q.,Robinson, H.,Li, J. (deposition date: 2012-03-05, release date: 2012-06-27, Last modification date: 2023-09-13) |
| Primary citation | Han, Q.,Robinson, H.,Li, J. Biochemical identification and crystal structure of kynurenine formamidase from Drosophila melanogaster. Biochem.J., 446:253-260, 2012 Cited by 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: 22690733DOI: 10.1042/BJ20120416 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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