| Attributes | Values |
|---|
| rdf:type
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| 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. (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
- 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)
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| Title
| - 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)
- Molekulární mod interakce rostlinné aminooxidasy s mechanismem založeným na inhibitoru 2-butin-1,4-diaminu (cs)
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| skos:prefLabel
| - 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)
- Molekulární mod interakce rostlinné aminooxidasy s mechanismem založeným na inhibitoru 2-butin-1,4-diaminu (cs)
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| skos:notation
| - RIV/61989592:15310/00:00000972!RIV09-MSM-15310___
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| http://linked.open...avai/riv/aktivita
| |
| http://linked.open...avai/riv/aktivity
| - P(GA203/97/0097), P(ME 153), P(VS96021), Z(MSM 153100010), Z(MSM 153100013)
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
| |
| http://linked.open...ai/riv/idVysledku
| - RIV/61989592:15310/00:00000972
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| http://linked.open...riv/jazykVysledku
| |
| http://linked.open.../riv/klicovaSlova
| - DIAMINE OXIDASE; ACTIVE-SITE; CRYSTAL-STRUCTURE; CATALYTIC CYCLE; COPPER; PEA; 1; 4-DIAMINO-2-BUTYNE; TOPAQUINONE; RESOLUTION; SUBSTRATE (en)
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| http://linked.open.../riv/klicoveSlovo
| |
| http://linked.open...odStatuVydavatele
| - DE - Spolková republika Německo
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| http://linked.open...ontrolniKodProRIV
| |
| http://linked.open...i/riv/nazevZdroje
| - European Journal of Biochemistry
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| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
| |
| http://linked.open...cetTvurcuVysledku
| |
| http://linked.open...vavai/riv/projekt
| |
| http://linked.open...UplatneniVysledku
| |
| http://linked.open...v/svazekPeriodika
| |
| http://linked.open...iv/tvurceVysledku
| - Lemr, Karel
- Šebela, Marek
- Frébort, Ivo
- Peč, Pavel
- Bellelli, A.
- Hirota, S.
- Svendsen, I.
- Yamauchi, O.
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| http://linked.open...n/vavai/riv/zamer
| |
| issn
| |
| number of pages
| |
| http://localhost/t...ganizacniJednotka
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