Han_2012_Biochem.J_446_253

Reference

Title : Biochemical identification and crystal structure of kynurenine formamidase from Drosophila melanogaster. - Han_2012_Biochem.J_446_253
Author(s) : Han Q , Robinson H , Li J
Ref : Biochemical Journal , 446 :253 , 2012
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 alpha/beta 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.

PubMedSearch : Han_2012_Biochem.J_446_253
PubMedID: 22690733
Gene_locus related to this paper: drome-CG9542

Related information

Inhibitor PMSF
Substrate PMSF    N-formylkynurenine
Gene_locus PMSF    N-formylkynurenine    drome-CG9542
Family PMSF    N-formylkynurenine    drome-CG9542    Kynurenine-formamidase
Structure PMSF    N-formylkynurenine    drome-CG9542    Kynurenine-formamidase    4E15    4E11    4E14

Citations formats

Han Q, Robinson H, Li J (2012)
Biochemical identification and crystal structure of kynurenine formamidase from Drosophila melanogaster.
Biochemical Journal 446 :253

Han Q, Robinson H, Li J (2012)
Biochemical Journal 446 :253