Interakce pent-2-yn-1,5-diaminu s rostlinnými aminoxidasami obsahujícími měď

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002286" target="_blank" >RIV/61989592:15310/04:00002286 - 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

Interaction of pent-2-yne-1,5-diamine with plant copper amine oxidases

Popis výsledku v původním jazyce

Plant copper-containing amine oxidases (EC 1.4.3.6) catalyze the oxidative deamination of biogenic amines, which are known as cellular regulators, to form the corresponding aldehydes, ammonia and hydrogen peroxide. The enzymes are dimeric proteins containing both cupric ion and topaquinone as cofactors in each of the two subunits. They have been localized in the cell wall. Thus their physiological role, except for that in the catabolism of amines, may be seen in connection with the production of hydrogen peroxide that is utilized in peroxidase-mediated reactions in this cell compartment1. Here we report a study on the reaction of grass pea (Lathyrus sativus, GPAO) and sainfoin (Onobrychis viciifolia, OVAO) amine oxidases with pent-2-yne-1,5-diamine (DAPY). DAPY reacted with the topaquinone cofactor and was only weakly oxidized. Prolonged incubations, however, resulted in irreversible inhibition of the enzymes. For GPAO and OVAO, the rates of inactivation of 0.1-0.3 min-1 were determine

Název v anglickém jazyce

Interaction of pent-2-yne-1,5-diamine with plant copper amine oxidases

Popis výsledku anglicky

Plant copper-containing amine oxidases (EC 1.4.3.6) catalyze the oxidative deamination of biogenic amines, which are known as cellular regulators, to form the corresponding aldehydes, ammonia and hydrogen peroxide. The enzymes are dimeric proteins containing both cupric ion and topaquinone as cofactors in each of the two subunits. They have been localized in the cell wall. Thus their physiological role, except for that in the catabolism of amines, may be seen in connection with the production of hydrogen peroxide that is utilized in peroxidase-mediated reactions in this cell compartment1. Here we report a study on the reaction of grass pea (Lathyrus sativus, GPAO) and sainfoin (Onobrychis viciifolia, OVAO) amine oxidases with pent-2-yne-1,5-diamine (DAPY). DAPY reacted with the topaquinone cofactor and was only weakly oxidized. Prolonged incubations, however, resulted in irreversible inhibition of the enzymes. For GPAO and OVAO, the rates of inactivation of 0.1-0.3 min-1 were determine

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

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

2004

Kód důvěrnosti údajů

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

Název periodika

Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica

ISSN

0232-0061

e-ISSN

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Svazek periodika

43

Číslo periodika v rámci svazku

S

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

275

Strana od-do

43-44

Kód UT WoS článku

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EID výsledku v databázi Scopus

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