Amine oxidases oxidase

Nonblue oxidases Amine oxidase Diamine oxidases Galactose oxidase Cytochrome c oxidase... [Pg.191]

The function of the metal site in the oxygen-dependent radical enzymes galactose oxidase, amine oxidases, ribonucleotide reductase, and cytochrome c oxidase is inter alia to bind 02 in their reduced forms and undergo the appropriate redox chemistry to generate a metal-bound, activated oxygen species of variable nature. [Pg.158]

Copper Liver and organ meats grains, legumes, nuts, seeds (esp. cocoa powder) Component of many enzymes, especially oxidases Amine oxidases Lysyl oxidases Cytochrome oxidase... [Pg.346]

ACYL-CoA DEHYDROGENASES ADENYLYLSULEATE REDUCTASE ALCOHOL OXIDASE AMINE OXIDASES d-AMINO acid DEHYDROGENASE l-AMINO acid DEHYDROGENASE d-AMINO ACID OXIDASE l-AMINO ACID OXIDASE d-ASPARTATE OXIDASE BENZOATE 1,2-DIOXYGENASE... [Pg.742]

Amine oxidases catalyze the oxidative deamination of both xenobiotic and biogenic amines, and thus have many critical biological functions. Two distinct classes differ in the nature of their prosthetic groups [1]. The flavin-(FAD flavin adenine dinucleotide)-dependent amine oxidases include monoamine oxidases (MAO A and B) and polyamine oxidases. Amine oxidases not containing FAD, the so-called semicarbazide-sensitive amine oxidases (SSAO), include both plasma amine oxidases and tissue amine oxidases. These contain quinonoid structures as redox cofactors that are derived from posttranslationally modified tyrosine or tryptophan side chains, topaoquinone frequently playing this role [2]. [Pg.662]

Oxidation galactose oxidase, amine oxidase, ascorbate oxidase, laccase, cytochrome c oxidase... [Pg.2]

Copper is an essential element to most life forms. In humans it is the third most abundant trace element only iron and zinc are present in higher quantity. Utilization of copper usually involves a protein active site which catalyzes a critical oxidation reaction, e.g., cytochrome oxidase, amine oxidases, superoxide dismutase, ferroxidases, dopamine-/ -hydrox-ylase, and tyrosinase. Accordingly, animals exhibit unique homeostatic mechanisms for the absorption, distribution, utilization, and excretion of copper (J). Moreover, at least two potentially lethal inherited diseases of copper metabolism are known Wilson s Disease and Menkes s Kinky Hair Syndrome (I). [Pg.265]

D-Aspartate oxidase L-Amino-acid oxidase D-Amino-acid oxidase Amine oxidase (flavin-containing) Amine oxidase (copper-containing) D-Glutamate oxidase Ethanolamine oxidase Putrescine oxidase L-Glutamate oxidase L-Lysine oxidase... [Pg.1389]

Ferrous oxidase Amine oxidase Zn Carbonic anhydrase... [Pg.2974]

In Cu compounds of high covalence no precise decision can be reached regarding the oxidation state of the copper (53), while in ionic systems reference to the occupancy of the 3d subshell is sufficient. Thus, the oxidation states given in I—IY are of merely formal nature. The interesting phenomenon in this scheme is the redox mesomerism of Cu which implies that the chelated metal ion could have different biochemical actions. Type I would represent the reversible oxygenation as found in haemo-cyanin, type II would be the superoxide dismutation, provided OI-really is the substrate, and types III and IV are represented by the catalatic and oxidative action displayed by a considerable number of copper proteins (polyphenol oxidases, amine oxidases etc.). The biochemical specificity of each chelated copper is more of less given by the macromolecular ligands. [Pg.50]

Examples Azurin Plastocyanin Stellacyanin Nitrite reductase Laccase Superoxide dismutase Galactose oxidase Amine oxidase Nitrite reductase Laccase Hemocyanin Tyrosinase Catechol oxidase Laccase Cyt c oxidase N2O reductase Menaquinol NO- reductase N2O reductase... [Pg.91]

Ascorbate oxidase Phenoxazinone synthase Galactose oxidase Amine oxidase... [Pg.2]

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