By Giovanni Floris, Bruno Mondovi

Although the volume of study on copper amine oxidases has grown quickly and considerably some time past decade, the sector regrettably suffers from loss of team spirit and demanding confusion surrounds features so simple as affirmation of enzyme identities. This e-book describes the constitution of the enzymes, the function of copper, and of the weird cofactor 6-hydroxydopa quinine derived from a posttranslational amendment of a tyrosine residue. It additionally covers the diversities of among AOs from micro organism, vegetation, and mammals. eventually, the textual content examines the significance of this ubiquitous category of enzymes in body structure and in metabolism of biogenic amines.

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This ability to stimulate glucose uptake is not a specific function of PrAO, since the hydrogen peroxide formed in the MAO-catalyzed reaction can do the same and we have no reason to suppose that other H2O2-forming enzymes may not do likewise. , 2007). , 2003). 2 Cell Death All these enzymes produce H2O2 as a product of amine oxidation. Although it is an important cellular signaling molecule, H2O2 is toxic at higher concentrations and linking it to cell death under pathophysiological conditions has become a popular pastime.

It is conceivable that the initial step in the oxidative half-reaction of Co(II) and Ni(II) AGAOs is the direct 1e – reduction of dioxygen from TPQaq and does not involve a change in the redox state of the metal. The initial reaction of TPQaq with O2 is much slower in Co(II) and Ni(II) AGAOs than in the native enzyme, and most likely is the rate-limiting step in the oxidative half-reaction of the metal-substituted enzymes. , 2003). The final step in the oxidative half-reaction under single turnover conditions is the hydrolysis of TPQimq to regenerate TPQox.

Other name(s): monoamine oxidase; tyramine oxidase; tyraminase; amine oxidase; adrenalin oxidase; epinephrine oxidase; MAO; serotonin deaminase; adrenaline oxidase; polyamine oxidase; spermidine oxidase; spermine oxidase. Systematic name: amine:oxygen oxidoreductase (deaminating) (flavin-containing). Comments: A flavoprotein (FAD). Acts on primary amines, and also on some secondary and tertiary amines. x, primary-amine oxidase, in oxidizing secondary and tertiary amines and inactivity toward methylamine.

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