Abstract Some structural and biochemical characteristics of polyamine oxidase (PAO) purified from maize shoots have been examined. The enzyme has only alanine as N- terminal amino acid and its N-terminal sequence shows a significant degree of homology with tryptophan 2-monooxygenase from Pseudomonas syringae pv. savastanoi. The pH optimum for the stability of the native enzyme is 5, similar to that of the barley leaf enzyme. ...
[Amatore, Christian; Badoz-Lambling, Janine; Bonnel-Huyghes, Claudine; Pinson, Jean; Saveant, Jean Michel; Thiebault, Andre Journal of the American Chemical Society, 1982 , vol. 104, # 7 p. 1979 - 1986]
