منابع مشابه
Biochemical identification and crystal structure of kynurenine formamidase from Drosophila melanogaster.
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, i...
متن کاملStructures of bacterial kynurenine formamidase reveal a crowded binuclear zinc catalytic site primed to generate a potent nucleophile
Tryptophan is an important precursor for chemical entities that ultimately support the biosynthesis of key metabolites. The second stage of tryptophan catabolism is catalysed by kynurenine formamidase, an enzyme that is different between eukaryotes and prokaryotes. In the present study, we characterize the catalytic properties and present the crystal structures of three bacterial kynurenine for...
متن کاملSynergistic and product induction of the enzymes of tryptophan metabolism in Pseudomonas acidovorans.
The process of induction of tryptophan oxygenase in Pseudomonas acidovorans is typical of many microbial enzyme induction systems, in that it (i) requires cell multiplication and de novo protein synthesis, (ii) is subject to catabolite repression, (iii) results in the formation of a stable enzyme, whose level, upon removal of inducer, is diluted out by cell proliferation, and (iv) exhibits prod...
متن کاملThe Kynurenine Pathway
The kynurenine pathway represents a major route for the catabolism of tryptophan (TRP). In the body, TRP is transported around the periphery either bound to albumin (90%) or in free form (10%), the two states existing in equilibrium (McMenamy 1965). However, only free form TRP can be transported across the blood-brain barrier (BBB) by the competitive and nonspecific L-type amino acid transporte...
متن کاملRegulatory Mechanisms Governing Synthesis of the Enzymes for Tryptophan Oxidation by Pseudomonas Fluorescens.
Both co-ordinate and sequential inductions govern the synthesis of the enzymes required for the oxidative dissimilation of L-tryptophan by a strain of Pseudomonas$zlorescerrs. The first two enzymes of the sequence, tryptophan pyrrolase and formylkynurenine formamidase, are induced co-ordinately by L-kynurenine, the product of their successive action on L-tryptophan; L-tryptophan itself is not a...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)42438-1