Copper-containing amine oxidases are found in bacteria, fungi, plants and animals. In prokaryotes, the enzyme enables various amine substrates to be used as sources of carbon and nitrogen.[3][4]
The copper amine oxidase 3-dimensional structure was determined through X-ray crystallography.[1]
The copper amine oxidases occur as mushroom-shaped homodimers of 70-95 kDa, each monomer containing a copper ion and a covalently bound redox cofactor, topaquinone (TPQ). TPQ is formed by post-translational modification of a conserved tyrosine residue. The copper ion is coordinated with three histidine residues and two water molecules in a distorted square pyramidal geometry, and has a dual function in catalysis and TPQ biogenesis. The catalytic domain is the largest of the 3-4 domains found in copper amine oxidases, and consists of a beta sandwich of 18 strands in two sheets. The active site is buried and requires a conformational change to allow the substrate access.
The N2 and N3 N-terminal domains share a common structural fold, its core consisting of alpha-beta(4), where the helix is packed against the coiled anti-parallel beta-sheets. An additional domain is found at the N-terminal of some copper amine oxidases, as well as in related proteins such as cell wallhydrolase and N-acetylmuramoyl-L-alanine amidase. This domain consists of a five-stranded antiparallel beta-sheet twisted around an alpha helix.[5][6]
In eukaryotes they have a broader range of functions, including cell differentiation and growth, wound healing, detoxification and cell signalling;[7] one AOC enzyme (AOC3) functions as a vascular adhesion protein (VAP-1) in some mammalian tissues.[1]
^Murray JM, Convery MA, Phillips SE, McPherson MJ, Knowles PF, Parsons MR, Wilmot CM, Blakeley V, Corner AS, Alton G, Palcic MM (1997). "Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction". Biochemistry. 36 (7): 1608–1620. doi:10.1021/bi962205j. PMID9048544.
^Tanizawa K, Guss JM, Freeman HC, Yamaguchi H, Wilce MC, Dooley DM, Matsunami H, Mcintire WS, Ruggiero CE (1997). "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. doi:10.1021/bi971797i. PMID9405045.
Mondovi B, Costa MT, Agro AF, Rotilio G (1967). "Pyridoxal phosphate as a prosthetic group of pig kidney diamine oxidase". Arch. Biochem. Biophys. 119 (1): 373–81. doi:10.1016/0003-9861(67)90468-7. PMID4964016.