Recombinant Danio rerio Kynurenine 3-Monooxygenase (KMO) is a recombinant protein derived from zebrafish, expressed in Escherichia coli (E. coli). This enzyme plays a crucial role in the kynurenine pathway, which is involved in tryptophan metabolism. KMO catalyzes the conversion of L-kynurenine to 3-hydroxykynurenine, a step that is significant in various biological processes, including neurodegenerative diseases and immune responses.
The recombinant full-length Danio rerio KMO protein is His-tagged and consists of 474 amino acids (1-474aa). It is expressed in E. coli and available in a lyophilized powder form. The protein has a purity of greater than 90% as determined by SDS-PAGE. Storage recommendations include maintaining it at -20°C or -80°C upon receipt, with aliquoting necessary for multiple uses to avoid repeated freeze-thaw cycles .
KMO is a key enzyme in the kynurenine pathway, which is involved in the breakdown of tryptophan. This pathway is crucial for various physiological processes and has been implicated in neurodegenerative diseases, cancer, and immune responses. The enzyme catalyzes the conversion of L-kynurenine to 3-hydroxykynurenine, which can further metabolize into quinolinic acid, a compound with neurotoxic properties .
Recent studies have highlighted the potential antiviral properties of KMO and its metabolites. For instance, quinolinic acid, a downstream product of KMO activity, has been shown to induce type I interferon production, thereby exerting broad-spectrum antiviral effects . While specific research on the recombinant Danio rerio KMO is limited, its role in tryptophan metabolism and potential applications in antiviral therapy make it an interesting subject for further investigation.
Function: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). This enzyme is essential for quinolinic acid biosynthesis.
STRING: 7955.ENSDARP00000024051
UniGene: Dr.79892