"Yamauchi, O." . "Byla studov\u00E1na interakce Cu-aminoxidasy s reak\u010Dn\u011B z\u00E1visl\u00FDm inhibitorem 1,4-diamino-2-butynem (DABY), kter\u00FD je analogem p\u0159\u00EDrodn\u00EDho substr\u00E1tu putrescinu (1,4-diaminobutan). DABY je substr\u00E1tem enzymu, ale p\u0159i jeho p\u0159em\u011Bn\u011B doch\u00E1z\u00ED k vzniku reaktivn\u00EDho intermedi\u00E1tu, kter\u00FD enzym ireverzibiln\u011B inaktivuje cestou tvorby pyrrolov\u00E9ho aduktu na postrann\u00EDm \u0159et\u011Bzci nukleofiln\u00ED aminokyseliny (Lys, Glu), kter\u00E1 je nepostradateln\u00E1 pro katalytick\u00FD mechanismus \u010Di transport substr\u00E1tu do aktivn\u00EDho m\u00EDsta. Princip inaktivace byl vysv\u011Btlen na z\u00E1klad\u011B v\u00FDsledk\u016F detailn\u00EDch instrument\u00E1ln\u00EDch experiment\u016F s vyu\u017Eit\u00EDm absorp\u010Dn\u00ED spektroskopie, chromatografie a hmotnostn\u00ED spektrometrie."@cs . . . . "2-Butyne-1,4-diamine (DABI) is a mechanism-based inhibitor of copper-containing plant amine oxidases; the number of turnovers that leads to enzyme inactivation is approximate to 20. The product of DABI oxidation is a very reactive aminoallene that reacts with an essential nucleophilic group at the enzyme active site, forming a covalently bound pyrrole and producing an inactive enzyme. The inactivated enzyme shows a new absorption maximum at 295 nm and gives coloured derivatives with p-dimethylaminobenzaldehyde and p dimethylaminocinnamaldehyde that are spectrally similar to the products of pyrrole treated with the above reagents. Resonance Raman spectra of the p-dimethylaminobenzaldehyde adduct of pyrrole and the inactivated enzyme show very high degree of similarity, supporting the idea that the product of inactivation is indeed a bound pyrrole. The bound pyrrole is formed already in the anaerobic step of the reaction, while the topa semiquinone radical is not affected, as shown by the EPR and stoppe"@en . "European Journal of Biochemistry" . . "RIV/61989592:15310/00:00000972" . "[CEC032054C78]" . . "Molekul\u00E1rn\u00ED mod interakce rostlinn\u00E9 aminooxidasy s mechanismem zalo\u017Een\u00FDm na inhibitoru 2-butin-1,4-diaminu"@cs . . . . . . "267" . "4"^^ . "Molekul\u00E1rn\u00ED mod interakce rostlinn\u00E9 aminooxidasy s mechanismem zalo\u017Een\u00FDm na inhibitoru 2-butin-1,4-diaminu"@cs . . . "P(GA203/97/0097), P(ME 153), P(VS96021), Z(MSM 153100010), Z(MSM 153100013)" . . "15310" . . . "Hirota, S." . "DE - Spolkov\u00E1 republika N\u011Bmecko" . "\u0160ebela, Marek" . "Fr\u00E9bort, Ivo" . "RIV/61989592:15310/00:00000972!RIV09-MSM-15310___" . "11"^^ . "717999" . "Svendsen, I." . . . . . "Molecular mode of interaction of plant amine oxidase with the mechanism-based inhibitor 2-butyne-1,4-diamine"@en . . "DIAMINE OXIDASE; ACTIVE-SITE; CRYSTAL-STRUCTURE; CATALYTIC CYCLE; COPPER; PEA; 1; 4-DIAMINO-2-BUTYNE; TOPAQUINONE; RESOLUTION; SUBSTRATE"@en . "2-Butyne-1,4-diamine (DABI) is a mechanism-based inhibitor of copper-containing plant amine oxidases; the number of turnovers that leads to enzyme inactivation is approximate to 20. The product of DABI oxidation is a very reactive aminoallene that reacts with an essential nucleophilic group at the enzyme active site, forming a covalently bound pyrrole and producing an inactive enzyme. The inactivated enzyme shows a new absorption maximum at 295 nm and gives coloured derivatives with p-dimethylaminobenzaldehyde and p dimethylaminocinnamaldehyde that are spectrally similar to the products of pyrrole treated with the above reagents. Resonance Raman spectra of the p-dimethylaminobenzaldehyde adduct of pyrrole and the inactivated enzyme show very high degree of similarity, supporting the idea that the product of inactivation is indeed a bound pyrrole. The bound pyrrole is formed already in the anaerobic step of the reaction, while the topa semiquinone radical is not affected, as shown by the EPR and stoppe" . . . "0014-2956" . . "5" . . "Pe\u010D, Pavel" . "Molecular mode of interaction of plant amine oxidase with the mechanism-based inhibitor 2-butyne-1,4-diamine" . "Molecular mode of interaction of plant amine oxidase with the mechanism-based inhibitor 2-butyne-1,4-diamine"@en . "Bellelli, A." . . . . . . "8"^^ . . "Lemr, Karel" . "Molecular mode of interaction of plant amine oxidase with the mechanism-based inhibitor 2-butyne-1,4-diamine" . .