. "\u0160ebela, Marek" . . "15310" . . "RIV/61989592:15310/04:00002286" . "275"^^ . . "Plant copper-containing amine oxidases (EC 1.4.3.6) catalyze the oxidative deamination of biogenic amines, which are known as cellular regulators, to form the corresponding aldehydes, ammonia and hydrogen peroxide. The enzymes are dimeric proteins containing both cupric ion and topaquinone as cofactors in each of the two subunits. They have been localized in the cell wall. Thus their physiological role, except for that in the catabolism of amines, may be seen in connection with the production of hydrogen peroxide that is utilized in peroxidase-mediated reactions in this cell compartment1. Here we report a study on the reaction of grass pea (Lathyrus sativus, GPAO) and sainfoin (Onobrychis viciifolia, OVAO) amine oxidases with pent-2-yne-1,5-diamine (DAPY). DAPY reacted with the topaquinone cofactor and was only weakly oxidized. Prolonged incubations, however, resulted in irreversible inhibition of the enzymes. For GPAO and OVAO, the rates of inactivation of 0.1-0.3 min-1 were determined, the apparent" . "Pe\u010D, Pavel" . "amine oxidase;diamine;mechanism-based inhibition;nuclear magnetic resonance;oxidation."@en . . "Interakce pent-2-yn-1,5-diaminu s rostlinn\u00FDmi aminoxidasami obsahuj\u00EDc\u00EDmi m\u011B\u010F"@cs . . "0232-0061" . . "RIV/61989592:15310/04:00002286!RIV/2005/MSM/153105/N" . "Interaction of pent-2-yne-1,5-diamine with plant copper amine oxidases" . . . . . "CZ - \u010Cesk\u00E1 republika" . . "Malo\u0148, Michal" . "43" . "Lenobel, Ren\u00E9" . "Interaction of pent-2-yne-1,5-diamine with plant copper amine oxidases"@en . "43-44" . "Z(MSM 153100010)" . "5"^^ . "Havli\u0161, Jan" . "S" . "Lamplot, Zbyn\u011Bk" . . . "8"^^ . . . "Lemr, Karel" . . . "Sayre, Lawrence M." . . "568558" . "Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica" . . "Plant copper-containing amine oxidases (EC 1.4.3.6) catalyze the oxidative deamination of biogenic amines, which are known as cellular regulators, to form the corresponding aldehydes, ammonia and hydrogen peroxide. The enzymes are dimeric proteins containing both cupric ion and topaquinone as cofactors in each of the two subunits. They have been localized in the cell wall. Thus their physiological role, except for that in the catabolism of amines, may be seen in connection with the production of hydrogen peroxide that is utilized in peroxidase-mediated reactions in this cell compartment1. Here we report a study on the reaction of grass pea (Lathyrus sativus, GPAO) and sainfoin (Onobrychis viciifolia, OVAO) amine oxidases with pent-2-yne-1,5-diamine (DAPY). DAPY reacted with the topaquinone cofactor and was only weakly oxidized. Prolonged incubations, however, resulted in irreversible inhibition of the enzymes. For GPAO and OVAO, the rates of inactivation of 0.1-0.3 min-1 were determined, the apparent"@en . "Interaction of pent-2-yne-1,5-diamine with plant copper amine oxidases" . "Interaction of pent-2-yne-1,5-diamine with plant copper amine oxidases"@en . "\u010Cl\u00E1nek se zab\u00FDv\u00E1 interakc\u00ED pent-2-yn-1,5-diaminu s rostlinn\u00FDmi aminoxidasami obsahuj\u00EDc\u00EDmi m\u011B\u010F."@cs . . "Interakce pent-2-yn-1,5-diaminu s rostlinn\u00FDmi aminoxidasami obsahuj\u00EDc\u00EDmi m\u011B\u010F"@cs . "[583CD37EEA61]" .