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
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DOI - Digital Object Identifier
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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
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Czech description
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Classification
Type
D - Article in proceedings
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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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
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ISSN
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e-ISSN
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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
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Type of event by nationality
EUR - Evropská akce
UT code for WoS article
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