Copper amine oxidases : structures, catalytic mechanisms, by Giovanni Floris, Bruno Mondovi

By Giovanni Floris, Bruno Mondovi

Although the volume of study on copper amine oxidases has grown speedily and considerably long ago decade, the sphere regrettably suffers from loss of harmony and important 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 variations of among AOs from micro organism, vegetation, and mammals. ultimately, the textual content examines the significance of this ubiquitous type of enzymes in body structure and in metabolism of biogenic amines.

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Additional info for Copper amine oxidases : structures, catalytic mechanisms, and role in pathophysiology

Sample text

Substrates that have been shown to be oxidized by SSAO and not by MAO include methylamine and aminoacetone. Thus, one of those might be used in a name, but that would tend to obscure the broad substrate specificity. , 1993). The most consistent difference between MAO and SSAO appears to be the ability of the former to catalyze the oxidation of secondary amines such as adrenaline and Nomenclature and Potential Functions of Copper Amine Oxidases 11 some tertiary amines. This can be used as a clear specificity difference to distinguish the enzymes.

The protein was kept through four changes of buffer. After dialysis against the second buffer, the Cu-depleted HPAO was removed from the Slide-a-Lyzer with a syringe. All buffers were degassed prior to use and phosphate buffer was passed through a column of chelating resin to avoid metal contamination. 1. The relative activities and residual Cu contents of Cu-depleted AOs indicate the difficulty of achieving complete Cu depletion from enzymes because of tight binding of Cu to the active site and some Cu contamination during the depletion processes.

Can pivot and rotate in the wedge cavity and can swing out of the wedge when it is freed from the hydrogen bond interaction with the conserved Tyr (Y284 in AGAO). , 1995). , 1997). 6b). The crystals in which TPQ is bound to Cu2+ are colorless, indicating charge localization of the O4 anion through ligation to Cu2+.

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