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Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification

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http://www.sciencedirect.com/science/article/pii/S1046592813002593
Original languageEnglish
Pages (from-to)96-103
Number of pages8
JournalProtein Expression and Purification
Volume95
DOIs
Publication statusPublished - Mar 2014

Abstract

Kynurenine 3-monooxygenase (KMO) is an enzyme central to the kynurenine pathway of tryptophan metabolism. KMO has been implicated as a therapeutic target in several disease states, including Huntington's disease. Recombinant human KMO protein production is challenging due to the presence of transmembrane domains, which localise KMO to the outer mitochondrial membrane and render KMO insoluble in many in vitro expression systems. Efficient bacterial expression of human KMO would accelerate drug development of KMO inhibitors but until now this has not been achieved. Here we report the first successful bacterial (Escherichia coli) expression of active FLAG™-tagged human KMO enzyme expressed in the soluble fraction and progress towards its purification.

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