Recent news related to substrates and inhibitors of plant copper amine oxidases

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F02%3A00001661" target="_blank" >RIV/61989592:15310/02:00001661 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Recent news related to substrates and inhibitors of plant copper amine oxidases

Popis výsledku v původním jazyce

Plant copper amine oxidases (CAOs; EC 1.4.3.6) belong to the quinoprotein family. Besides the cofactor topaquinone, they also contain cupric ions participating in the reaction. Numerous substrates and inhibitors of plant CAOs have been reported up to date. We studied interactions of pea seedling enzyme (PSAO) with several artificial amine compounds that have not yet been analysed in this way and whose structure mimic natural polyamine substrates. In addition, our attention was paid to the evaluation ofinhibition potency of sedamine alkaloids and various pyridine-derived oximes. 1,4-Bis(3-aminopropyl)piperazine, N,N´-bis(3-aminopropyl)-trans-2-butene-1,4-diamine and 3-oxapentane-1,5-diamine (OPD) were found to be substrates of PSAO. The corresponding enzyme kinetics was measured, the reaction stoichiometry analysed and rapid-scanning spectrophotometry applied to investigate the reaction mechanism. The identity of the main product of OPD conversion was confirmed by several analytical me

Název v anglickém jazyce

Recent news related to substrates and inhibitors of plant copper amine oxidases

Popis výsledku anglicky

Plant copper amine oxidases (CAOs; EC 1.4.3.6) belong to the quinoprotein family. Besides the cofactor topaquinone, they also contain cupric ions participating in the reaction. Numerous substrates and inhibitors of plant CAOs have been reported up to date. We studied interactions of pea seedling enzyme (PSAO) with several artificial amine compounds that have not yet been analysed in this way and whose structure mimic natural polyamine substrates. In addition, our attention was paid to the evaluation ofinhibition potency of sedamine alkaloids and various pyridine-derived oximes. 1,4-Bis(3-aminopropyl)piperazine, N,N´-bis(3-aminopropyl)-trans-2-butene-1,4-diamine and 3-oxapentane-1,5-diamine (OPD) were found to be substrates of PSAO. The corresponding enzyme kinetics was measured, the reaction stoichiometry analysed and rapid-scanning spectrophotometry applied to investigate the reaction mechanism. The identity of the main product of OPD conversion was confirmed by several analytical me

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F00%2FD119" target="_blank" >GA203/00/D119: Studium struktury a vlastností endogenního inhibitoru aminoxidasy ze semenáčků fazolu a jeho analog</a><br>

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

30rd International Symposium on Vitamin B6, PQQ, Carbonyl Catalysis and quinoproteins

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

60

Strana od-do

37

Název nakladatele

University of Southampton

Místo vydání

Southampton

Místo konání akce

Southampton

Datum konání akce

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Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

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