Výskyt a lokalizace aktivity aminoaldehyddehydrogenasy v rostlinách Poaceae a Fabaceae

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002191" target="_blank" >RIV/61989592:15310/04:00002191 - 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

Occurence and localisation of aminoaldehyde dehydrogenase activity in Poaceae and Fabaceae plants

Popis výsledku v původním jazyce

Polyamines are regulatory substances involved in key developmental processes1,2. The catabolic regulation of polyamines is mediated by quinoprotein Cu-amine oxidases (Cu-AOs; EC1.4.3.6) and flavoprotein FAD-polyamine oxidases (PAOs; EC 1.5.3.-)2,3. In plants, these enzymes produce aminoaldehydes, which are further metabolised by NAD+-dependent aminoaldehyde dehydrogenases (AMADHs, EC 1.2.1.19 or 1.2.1.54). AMADHs have been found in legumes and grasses4, the enzymes from pea and oats were purified to homogeneity and characterised5,6. Pea AMADH has been localised in tissues of etiolated seedlings using histochemistry7. Here we report a screening study directed to the occurrence of AMADH in various plant species belonging to legumes (Fabaceae) and grasses(Poaceae). Fenugreek was chosen as a legume, the cereals barley, maize, oats, rye, triticale and wheat were representatives of grasses. 3-Aminopropionaldehyde (APAL) served as a substrate for AMADH assay. Activity level of the enzyme was

Název v anglickém jazyce

Occurence and localisation of aminoaldehyde dehydrogenase activity in Poaceae and Fabaceae plants

Popis výsledku anglicky

Polyamines are regulatory substances involved in key developmental processes1,2. The catabolic regulation of polyamines is mediated by quinoprotein Cu-amine oxidases (Cu-AOs; EC1.4.3.6) and flavoprotein FAD-polyamine oxidases (PAOs; EC 1.5.3.-)2,3. In plants, these enzymes produce aminoaldehydes, which are further metabolised by NAD+-dependent aminoaldehyde dehydrogenases (AMADHs, EC 1.2.1.19 or 1.2.1.54). AMADHs have been found in legumes and grasses4, the enzymes from pea and oats were purified to homogeneity and characterised5,6. Pea AMADH has been localised in tissues of etiolated seedlings using histochemistry7. Here we report a screening study directed to the occurrence of AMADH in various plant species belonging to legumes (Fabaceae) and grasses(Poaceae). Fenugreek was chosen as a legume, the cereals barley, maize, oats, rye, triticale and wheat were representatives of grasses. 3-Aminopropionaldehyde (APAL) served as a substrate for AMADH assay. Activity level of the enzyme was

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

53-55

Kód UT WoS článku

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EID výsledku v databázi Scopus

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