amine oxidase (pyridoxal containing) (incorrect)
semicarbazide-sensitive amine oxidase (ambiguous)
Glycine, serine and threonine metabolism
Substrate Schiff-base (Iminoquinone=substrate)
Product Schiff-base (Aminoquinol=product)
HIS 442;HIS 444;HIS 603(Copper);ASP 451;PHE 452;ASP 453;ASP 592;ILE 593(Manganese)
Stereochemical trends in copper amine oxidase reactions.
A Cu(I)-semiquinone state in substrate-reduced amine oxidases.
A substrate-cofactor free radical intermediate in the reaction mechanism of copper amine oxidase.
Purification and characterization of pea seedling amine oxidase for crystallization studies.
The reaction mechanism of copper amine oxidase: detection of intermediates by the use of substrates and inhibitors.
Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 A resolution.
Visualization of dioxygen bound to copper during enzyme catalysis.
Molecular mode of interaction of plant amine oxidase with the mechanism-based inhibitor 2-butyne-1,4-diamine.
Agmatine oxidation by copper amine oxidase.
Towards the development of selective amine oxidase inhibitors. Mechanism-based inhibition of six copper containing amine oxidases.
Differential inhibition of six copper amine oxidases by a family of 4-(aryloxy)-2-butynamines: evidence for a new mode of inactivation.
A theoretical study of the mechanism for the biogenesis of cofactor topaquinone in copper amine oxidases.
Using xenon as a probe for dioxygen-binding sites in copper amine oxidases.
The catalytic domain of this enzyme is homologous to those of counterpart enzymes from E. coli (M00103 in EzCatDB), and from bovine (T00251 in EzCatDB). Cofactor, topaquinone (2,4,5-trihydroxyphenylalanine), is a modified residue, generated from active site tyrosine residue (Tyr466) by self-catalysis (see [6] of M00103 in EzCatDB). Although this enzyme binds a copper ion and a manganese ion as cofactors per subunit, the manganese ion is not involved in catalysis. According to the literature [6] and [7] (for its homologue), this enzyme catalyzes two half-reactions: (I) reductive half-reaction, and (II) oxidative half-reaction. These half-reactions can be subdivided into several basic reactions in terms of RLCP classification. (I) Reductive half-reaction: (A) Exchange of double-bonded atoms; Schiff-base formation; Substrate amine forms a Schiff-base with topaquinone, generating iminoquinone=substrate and H2O (dehydration): (B) Isomerization from iminoquinone=substrate complex to aminoquinol=product complex (through a carbanionic intermediate): (C) Exchange of double-bonded atoms; Schiff-base deformation; H2O reacts with the intermediate, generating aminoquinol and product aldehyde (hydration): (II) Oxidative half-reaction: (D) Reduction of dioxygen (O2) by aminoquinol, to produce hydrogen peroxide (H2O2) and iminoquinone (Hydride transfer): (E) Exchange of double-bonded atoms; Schiff-base deformation; H2O reacts with the intermediate, generating topaquinone and product ammonia (hydration):