Mure, MinaeMoore, Robyn Haley2009-11-022009-11-022009-06-162009http://dissertations.umi.com/ku:10438https://hdl.handle.net/1808/5568Copper amine oxidases (CAOs) are essential for maintaining the level of biogenic amines in the body as well as being involved in the inflammation and immune responses. Lysyl oxidase (LOX), a member of CAO, plays an important role in stabilizing the extracellular matrix but its over-expression has been associated with metastasis/invasion of breast cancer cells. The biogeneses of the topaquinone (TPQ) cofactor of CAO and the lysine tyrosylquinone (LTQ) cofactor in LOX from the corresponding Tyr residue are self-catalyzed processes requiring copper and O2. In CAO, a putative dopaquinone (DPQ) intermediate has been proposed to react with a copper-associated water molecule, through a 1,4-addition mechanism, leading to the formation of TPQ. The D298K mutant of a bacterial CAO produces an iminoquinone tautomer (LTI) of lysine tyrosylquinone (LTQ). The results of this study strongly support the proposal that DPQ is a common intermediate in the biogenesis of these tyrosine-derived cofactors.152 pagesENThis item is protected by copyright and unless otherwise specified the copyright of this thesis/dissertation is held by the author.Organic chemistryLtqQuinone cofactorTpqDissertationopenAccess