"Havlis, J." . . . "4696-4708" . "13"^^ . "RIV/61989592:15310/04:00002169!RIV/2005/MSM/153105/N" . "1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases"@en . "1,5-Diamino-2-pentyne (DAPY) was found to be a weak substrate of grass pea (Lathyrus sativus, GPAO) and sainfoin (Onobrychis viciifolia, OVAO) amine oxidases. Prolonged incubations, however, resulted in irreversible inhibition of both enzymes. For GPAO and OVAO, rates of inactivation of 0.1-0.3 min(-1) were determined, the apparent K-I values (half-maximal inactivation) were of the order of 10(-5) M. DAPY was found to be a mechanism-based inhibitor of the enzymes because the substrate cadaverine significantly prevented irreversible inhibition. The N-1-methyl and N-5-methyl analogs of DAPY were tested with GPAO and were weaker inactivators (especially the N-5-methyl) than DAPY. Prolonged incubations of GPAO or OVAO with DAPY resulted in the appearance of a yellow-brown chromophore (lambda(max) = 310-325 nm depending on the working buffer). Excitation at 310 nm was associated with emitted fluorescence with a maximum at 445 nm, suggestive of extended conjugation. After dialysis, the color intensity was s"@en . "0014-2956" . "1,5-diamino-2-pentin je substr\u00E1tem i inaktiv\u00E1torem rostlinn\u00E9 Cu aminooxidasy"@cs . "1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases"@en . "Pe\u010D, Pavel" . . "Bylo zji\u0161t\u011Bno, \u017Ee 1,5-diamino-2-pentin je substr\u00E1tem i inaktiv\u00E1torem rostlinn\u00E9 Cu aminooxidasy."@cs . "Lenobel, Ren\u00E9" . "\u0160ebela, Marek" . . "271" . "1,5-diamino-2-pentin je substr\u00E1tem i inaktiv\u00E1torem rostlinn\u00E9 Cu aminooxidasy"@cs . "596529" . . . . "[E98821BE28E8]" . . . "23-24" . "1,5-Diamino-2-pentyne (DAPY) was found to be a weak substrate of grass pea (Lathyrus sativus, GPAO) and sainfoin (Onobrychis viciifolia, OVAO) amine oxidases. Prolonged incubations, however, resulted in irreversible inhibition of both enzymes. For GPAO and OVAO, rates of inactivation of 0.1-0.3 min(-1) were determined, the apparent K-I values (half-maximal inactivation) were of the order of 10(-5) M. DAPY was found to be a mechanism-based inhibitor of the enzymes because the substrate cadaverine significantly prevented irreversible inhibition. The N-1-methyl and N-5-methyl analogs of DAPY were tested with GPAO and were weaker inactivators (especially the N-5-methyl) than DAPY. Prolonged incubations of GPAO or OVAO with DAPY resulted in the appearance of a yellow-brown chromophore (lambda(max) = 310-325 nm depending on the working buffer). Excitation at 310 nm was associated with emitted fluorescence with a maximum at 445 nm, suggestive of extended conjugation. After dialysis, the color intensity was s" . . "European Journal of Biochemistry" . . "Malo\u0148, Michal" . . "DE - Spolkov\u00E1 republika N\u011Bmecko" . . . "15310" . "Sayre, L. M." . . . "Z(MSM 153100010)" . . "RIV/61989592:15310/04:00002169" . . "Lamplot, Z." . "Lemr, Karel" . . "5"^^ . . "1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases" . "Qiao, CH." . "9"^^ . . "amine oxidase;diamine;mechanism-based inhibition;nuclear magnetic resonance;oxidation"@en . "1,5-diamino-2-pentyne is both a substrate and inactivator of plant copper amine oxidases" .