Development in the course of study substrates and inhibitors of plant copper amine oxidases

Kód výsledku v IS VaVaI

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Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Development in the course of study substrates and inhibitors of plant copper amine oxidases

Popis výsledku v původním jazyce

Plant copper amine oxidases (CuAOS; EC 1. 4. 3. 6) belong to the quinoprotein family. Besides the cofactor topaquinone, they also contain cupric ions participating in the reaction. They catalyse the oxidative deamination of amine substrates to the respective aldehydes, ammonia and hydrogen peroxide (MEDDA, 1995). We studied interactions of pea seedling enzyme (PSAO) with several artifical amine compounds that have not yet been analysed in this way and whose structure mimic natural polyamine substrates.In the second part we focused our attention on the interaction of optically active sedamine alkaloids and various pyridine-derived oximes with PSAO. 3-Oxapentane-1,5-diamine (OPD), 1, 4-bis-(3-aminopropyl)piperazine and N, N-bis(3-aminopropyl)-trans-2-butene were found to be substrates of PSAO. The corresponding enzyme kinetics was measured, the reaction stechiometry analysed and rapid scanning spectrophotometry applied to investigate the reaction mechanism. A similar compound to OPD, 3-

Název v anglickém jazyce

Development in the course of study substrates and inhibitors of plant copper amine oxidases

Popis výsledku anglicky

Plant copper amine oxidases (CuAOS; EC 1. 4. 3. 6) belong to the quinoprotein family. Besides the cofactor topaquinone, they also contain cupric ions participating in the reaction. They catalyse the oxidative deamination of amine substrates to the respective aldehydes, ammonia and hydrogen peroxide (MEDDA, 1995). We studied interactions of pea seedling enzyme (PSAO) with several artifical amine compounds that have not yet been analysed in this way and whose structure mimic natural polyamine substrates.In the second part we focused our attention on the interaction of optically active sedamine alkaloids and various pyridine-derived oximes with PSAO. 3-Oxapentane-1,5-diamine (OPD), 1, 4-bis-(3-aminopropyl)piperazine and N, N-bis(3-aminopropyl)-trans-2-butene were found to be substrates of PSAO. The corresponding enzyme kinetics was measured, the reaction stechiometry analysed and rapid scanning spectrophotometry applied to investigate the reaction mechanism. A similar compound to OPD, 3-

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2002

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název statě ve sborníku

18th Joint Congress of the Czech and Slovak Societies for Biochemistry and Molecular Biology

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

410

Strana od-do

110

Název nakladatele

Slovenská spoločnosť pre biochémiu a molekulárnu biológiu

Místo vydání

Bratislava

Místo konání akce

Stará Lesná

Datum konání akce

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Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

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