|PROSITE documentation PDOC00895 [for PROSITE entry PS01165]|
Amine oxidases (AO)  are enzymes that catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing (EC 22.214.171.124) and copper-containing (EC 126.96.36.199).
Copper-containing AO is found in bacteria, fungi, plants and animals, it is an homodimeric enzyme that binds one copper ion per subunit as well as a 2,4,5-trihydroxyphenylalanine quinone (or topaquinone) (TPQ) cofactor. This cofactor is derived from a tyrosine residue.
We have derived two signature patterns for copper AO, the first one contains the tyrosine which give rises to the TPQ cofactor while the second one contains one of the three histidines that bind the copper atom .Last update:
July 1999 / Patterns and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Knowles P.F. Dooley D.M.|
|Source||(In) Metal ions in biological systems; Sigel H., Sigel A., Eds., 30:361- 403, Marcel Dekker, New-York, (1993).|
|2||Authors||Parsons M.R. Convery M.A. Wilmot C.M. Yadav K.D.S. Blakeley V. Corner A.S. Phillips S.E.V. McPherson M.J. Knowles P.F.|
|Title||Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.|