Purification and properties of diamine oxidase from Euphorbia latex.
A diamine oxidase has been purified to homogeneity from the latex of an herbaceous shrub, Euphorbia characias. This enzyme has a relative molecular mass of 144,000 and is composed of two identical subunits. It contain two Cu(II) and two carbonyl-like groups per dimer. The purified enzyme is pink and shows a broad absorption in the visible region centered at 480 nm, which is modified by the addition of phenylhydrazine or semicarbazide. The electron paramagnetic resonance spectrum is typical of copper(II) in a tetragonal symmetry. This enzyme oxidizes putrescine and cadaverine at fairly high rate and, less efficiently a few related compounds, but not histamine, spermine or spermidine.
D006631:Amine Oxidase (Copper-Containing) / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*; D013053:Spectrophotometry; D013379:Substrate Specificity
D006631:Amine Oxidase (Copper-Containing)