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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F00%3A00000972%21RIV09-MSM-15310___
rdf:type
skos:Concept n16:Vysledek
dcterms:description
Byla studována interakce Cu-aminoxidasy s reakčně závislým inhibitorem 1,4-diamino-2-butynem (DABY), který je analogem přírodního substrátu putrescinu (1,4-diaminobutan). DABY je substrátem enzymu, ale při jeho přeměně dochází k vzniku reaktivního intermediátu, který enzym ireverzibilně inaktivuje cestou tvorby pyrrolového aduktu na postranním řetězci nukleofilní aminokyseliny (Lys, Glu), která je nepostradatelná pro katalytický mechanismus či transport substrátu do aktivního místa. Princip inaktivace byl vysvětlen na základě výsledků detailních instrumentálních experimentů s využitím absorpční spektroskopie, chromatografie a hmotnostní spektrometrie. 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 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
dcterms:title
Molekulární mod interakce rostlinné aminooxidasy s mechanismem založeným na inhibitoru 2-butin-1,4-diaminu 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
skos:prefLabel
Molekulární mod interakce rostlinné aminooxidasy s mechanismem založeným na inhibitoru 2-butin-1,4-diaminu 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
skos:notation
RIV/61989592:15310/00:00000972!RIV09-MSM-15310___
n3:aktivita
n11:Z n11:P
n3:aktivity
P(GA203/97/0097), P(ME 153), P(VS96021), Z(MSM 153100010), Z(MSM 153100013)
n3:cisloPeriodika
5
n3:dodaniDat
n19:2009
n3:domaciTvurceVysledku
n8:4536274 n8:5433851 n8:9708790 n8:4316851
n3:druhVysledku
n18:J
n3:duvernostUdaju
n10:S
n3:entitaPredkladatele
n12:predkladatel
n3:idSjednocenehoVysledku
717999
n3:idVysledku
RIV/61989592:15310/00:00000972
n3:jazykVysledku
n15:eng
n3:klicovaSlova
DIAMINE OXIDASE; ACTIVE-SITE; CRYSTAL-STRUCTURE; CATALYTIC CYCLE; COPPER; PEA; 1; 4-DIAMINO-2-BUTYNE; TOPAQUINONE; RESOLUTION; SUBSTRATE
n3:klicoveSlovo
n7:COPPER n7:PEA n7:RESOLUTION n7:4-DIAMINO-2-BUTYNE n7:DIAMINE%20OXIDASE n7:CRYSTAL-STRUCTURE n7:CATALYTIC%20CYCLE n7:SUBSTRATE n7:ACTIVE-SITE n7:TOPAQUINONE n7:1
n3:kodStatuVydavatele
DE - Spolková republika Německo
n3:kontrolniKodProRIV
[CEC032054C78]
n3:nazevZdroje
European Journal of Biochemistry
n3:obor
n9:CE
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
8
n3:projekt
n5:GA203%2F97%2F0097 n5:VS96021 n5:ME%20153
n3:rokUplatneniVysledku
n19:2000
n3:svazekPeriodika
267
n3:tvurceVysledku
Yamauchi, O. Hirota, S. Šebela, Marek Frébort, Ivo Svendsen, I. Peč, Pavel Bellelli, A. Lemr, Karel
n3:zamer
n17:MSM%20153100013 n17:MSM%20153100010
s:issn
0014-2956
s:numberOfPages
11
n13:organizacniJednotka
15310