Pea seedling aminoaldehyde dehydrogenase: primary structure and active site residues

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15410%2F03%3A00001326" target="_blank" >RIV/61989592:15410/03:00001326 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15310/03:00001326

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 and active site residues

Popis výsledku v původním jazyce

The first primary structure of a plant aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.19) is reported. The enzyme of pea (Pisum sativum) seedlings subjected to our study oxidises omega-aminoaldehydes to the corresponding omega-amino acids. Although pea does not accumulate betaine aldehyde as a compatible osmolyte, the N-terminal sequence of a purified pea AMADH resembles those of plant betaine aldehyde dehydrogenases (BADHs). On the basis of an anticipated pea AMADH homology to these enzymes, degeneratedoligonucleotide primers were designed and used for PCR amplification. Two cDNA fragments were obtained in initial 5'RACE experiments. Subsequent 5' and 3' RACE performed with specific non-degenerated primers provided two putative cDNAs of the plant BADHfamily. Both encoded protein sequences (AMADH I and AMADH2) are highly homologous to those of plant BADHs. They show 81% identity and 92% in mutual alignment. As a deduced product of the first cDNA, AMADH1 completely matches the N-termina

Název v anglickém jazyce

Pea seedling aminoaldehyde dehydrogenase: primary structure and active site residues

Popis výsledku anglicky

The first primary structure of a plant aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.19) is reported. The enzyme of pea (Pisum sativum) seedlings subjected to our study oxidises omega-aminoaldehydes to the corresponding omega-amino acids. Although pea does not accumulate betaine aldehyde as a compatible osmolyte, the N-terminal sequence of a purified pea AMADH resembles those of plant betaine aldehyde dehydrogenases (BADHs). On the basis of an anticipated pea AMADH homology to these enzymes, degeneratedoligonucleotide primers were designed and used for PCR amplification. Two cDNA fragments were obtained in initial 5'RACE experiments. Subsequent 5' and 3' RACE performed with specific non-degenerated primers provided two putative cDNAs of the plant BADHfamily. Both encoded protein sequences (AMADH I and AMADH2) are highly homologous to those of plant BADHs. They show 81% identity and 92% in mutual alignment. As a deduced product of the first cDNA, AMADH1 completely matches the N-termina

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F99%2FD048" target="_blank" >GA203/99/D048: Purifikace rostlinné aminoaldehyddehydrogenasy a její enzymologická charakterizace</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2003

Kód důvěrnosti údajů

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

Název periodika

Plant Physiology and Biochemistry

ISSN

0981-9428

e-ISSN

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Svazek periodika

41

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

FR - Francouzská republika

Počet stran výsledku

10

Strana od-do

1-10

Kód UT WoS článku

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EID výsledku v databázi Scopus

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