Studies on the reaction of plant copper amine oxidase with the mechanism-based inhibitor 2-butyne-1,4diamine and other related diamines

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

Studies on the reaction of plant copper amine oxidase with the mechanism-based inhibitor 2-butyne-1,4diamine and other related diamines

Popis výsledku v původním jazyce

The reaction of grass pea amine oxidase (GPAO) with several aliphatic diamines, which have been reported as mechanism-based inhibitors of copper-containing amine oxidases (Cu-AOs), was studied. Kinetic measurements confirmed that (E)-2-butene-1,4-diamine(TDABE) and (Z)-2-butene-1,4-diamine (CDABE) could be classified as good substrates of GPAO. On the other hand, 2-butyne-1,4-diamine (DABI) was a poor substrate and propane-1,3-diamine (DAP) was not oxidized at all during the kinetic study. The irreversible activity loss occurred only after the reaction of GPAO with an excess of DABI, where an existence of covalent labeling of the enzyme could be demonstrated by chromatofocusing. Differential pulse polarography (DPP) was applied for detection of free aminoaldehydes as the products of the oxidative deamination. The results of DPP confirmed that only the oxidation product of DABI attacks the enzyme and its concentration in the reaction mixture slowly decreases. The reaction of pea aminoa

Název v anglickém jazyce

Studies on the reaction of plant copper amine oxidase with the mechanism-based inhibitor 2-butyne-1,4diamine and other related diamines

Popis výsledku anglicky

The reaction of grass pea amine oxidase (GPAO) with several aliphatic diamines, which have been reported as mechanism-based inhibitors of copper-containing amine oxidases (Cu-AOs), was studied. Kinetic measurements confirmed that (E)-2-butene-1,4-diamine(TDABE) and (Z)-2-butene-1,4-diamine (CDABE) could be classified as good substrates of GPAO. On the other hand, 2-butyne-1,4-diamine (DABI) was a poor substrate and propane-1,3-diamine (DAP) was not oxidized at all during the kinetic study. The irreversible activity loss occurred only after the reaction of GPAO with an excess of DABI, where an existence of covalent labeling of the enzyme could be demonstrated by chromatofocusing. Differential pulse polarography (DPP) was applied for detection of free aminoaldehydes as the products of the oxidative deamination. The results of DPP confirmed that only the oxidation product of DABI attacks the enzyme and its concentration in the reaction mixture slowly decreases. The reaction of pea aminoa

Druh

C - Kapitola v odborné knize

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

2000

Kód důvěrnosti údajů

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

Název knihy nebo sborníku

29th Annual Meeting of the European Histamine Research Society

ISBN

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Počet stran výsledku

97

Strana od-do

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Počet stran knihy

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Název nakladatele

European Histamine Research Society

Místo vydání

Rome, Italy

Kód UT WoS kapitoly

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