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

The result's identifiers

  • Result code in 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>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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

  • Czech name

  • Czech description

Classification

  • Type

    D - Article in proceedings

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2002

  • Confidentiality

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

Data specific for result type

  • Article name in the collection

    18th Joint Congress of the Czech and Slovak Societies for Biochemistry and Molecular Biology

  • ISBN

  • ISSN

  • e-ISSN

  • Number of pages

    410

  • Pages from-to

    147

  • Publisher name

    Slovenská spoločnosť pre biochémiu a molekulárnu biológiu

  • Place of publication

    Slovakia

  • Event location

    Stará Lesná

  • Event date

  • Type of event by nationality

    EUR - Evropská akce

  • UT code for WoS article