Plasma amine oxidase (PAO) catalyzes the reaction: RCH2NH2 + O2 + H2O → RCHO + NH3 + H2O2 Bovine plasma amine oxidase has a molecular weight of 170 kDa and an optimum pH of 6.2 for spermine and 7.2 for spermidine. Amine oxidases are divided into two classes: the pyridoxal and copper containing enzyme to which plasma amine oxidase belongs, and the FAD-containing amino oxidases. Natural substrates include catecholamines, tryptamine derivatives and other physiologically active amines. Plasma amine oxidase is used in research requiring nitrogen group transfers. The molecule is composed of two identical polypeptide chains. There are two pyridoxal phosphates and two atoms of Cu+ per molecule. Bovine plasma amine oxidase is inhibited by copper chelating agents, many carboxyl reagents such as cuprizone, hydroxylamine and cyanide. Benzoic acid and benzyl alcohol are both non-competitive inhibitors (KI = 30 and 34mM respectively).
Biochem/physiol Actions：
Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia. Has a preference for the primary monoamines methylamine and benzylamine. Could also act on 2-phenylethylamine but much less efficiently. At endothelial cells surface can also function as a cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion.
One unit results in the oxidation of one micromole of benzylamine per minute at 25°C, pH 7.2. under the specified conditions. 4,330 Tabor units is equivalent to one International Unit.
I2301744
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