Amine Oxidase (Arthrobacter strain FB24, recombinant)

Arthrobacter amine oxidase is a copper-dependent amine oxidase.¹ It exists as a homodimer and uses topaquinone as a cofactor.² Amine oxidase catalyzes the oxidation of a primary amine to a carbonyl resulting in the production of ammonia and hydrogen peroxide.^2,3 It has broad substrate specificity, oxidizing substrates such as tyramine, histamine, hexylamine, and agmatine, as well as herbicide-derived amines.^1,3 Amine oxidase has been used in a coupled-enzyme assay to measure phosphatidylethanolamine levels in isolated human plasma.¹ Cayman’s Amine Oxidase (Arthrobacter strain FB24, recombinant) protein contains a His-tag followed by a thrombin cleavage site and can be used for enzyme activity assay and Western blot (WB) applications.

WARNING This product is not for human or veterinary use.

1. Ota, H., Tamezane, H., Sasano, Y., et al. Enzymatic characterization of an amine oxidase from Arthrobacter sp. used to measure phosphatidylethanolamine. Biosci. Biotechnol. Biochem. 72(10), 2732-2738 (2008).

2. Wilce, M.C., Dooley, D.M., Freeman, H.C., et al. Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: Implications for the biogenesis of topaquinone. Biochemistry 36(51), 16116-16133 (1997).

3. Shapir, N., Monogodin, E.F., Sadowsky, M.J., et al. Evolution of catabolic pathways: Genomic insights into microbial s-triazine metabolism. J. Bacteriol. 189(3), 674-682 (2007).