Pea seedling aminoaldehyde dehydrogenase: Primary structure from protein and cDNA sequencing

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F02%3A00001428" target="_blank" >RIV/61989592:15310/02:00001428 - 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

Pea seedling aminoaldehyde dehydrogenase: Primary structure from protein and cDNA sequencing

Popis výsledku v původním jazyce

The first primary structure of a plant aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.18) from pea (Pisum sativum) was found. The studied enzyme belongs to the group of NAD+-dependent dehydrogenases. It catalyses oxidation of aminoaldehydes, which are formed by oxidative deamination of polyamines by the activity of amine oxidases (AO, EC 1.4.3.6.), to the corresponding amino acids. Although purified pea AMADH did not oxidise betaine aldehyde at all, its N-terminal amino acid sequence resembles those of various plant betaine aldehyde dehydrogenases (BADHs, EC 1.2.1.8) [ŠEBELA et al., 2000]. Plant BADHs are known as intracellular enzymes catalysing oxidation of betaine aldehyde - the second step of the formation of glycine betaine [WERETILNYK & HANSON, 1990]. Glycine betaine is known as a compatible osmolyte accumulated in some plant species (but surprisingly not in pea) in response to increased environmental salinity and draught [NUCCIO et al., 1999]. By assumed homology with BADH genes f

Název v anglickém jazyce

Pea seedling aminoaldehyde dehydrogenase: Primary structure from protein and cDNA sequencing

Popis výsledku anglicky

The first primary structure of a plant aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.18) from pea (Pisum sativum) was found. The studied enzyme belongs to the group of NAD+-dependent dehydrogenases. It catalyses oxidation of aminoaldehydes, which are formed by oxidative deamination of polyamines by the activity of amine oxidases (AO, EC 1.4.3.6.), to the corresponding amino acids. Although purified pea AMADH did not oxidise betaine aldehyde at all, its N-terminal amino acid sequence resembles those of various plant betaine aldehyde dehydrogenases (BADHs, EC 1.2.1.8) [ŠEBELA et al., 2000]. Plant BADHs are known as intracellular enzymes catalysing oxidation of betaine aldehyde - the second step of the formation of glycine betaine [WERETILNYK & HANSON, 1990]. Glycine betaine is known as a compatible osmolyte accumulated in some plant species (but surprisingly not in pea) in response to increased environmental salinity and draught [NUCCIO et al., 1999]. By assumed homology with BADH genes f

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

147

Název nakladatele

Slovenská spoločnosť pre biochémiu a molekulárnu biológiu

Místo vydání

Slovakia

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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