About: Pea seedling aminoaldehyde dehydrogenase: primary structure and active site residues

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	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, degenerated oligonucleotide 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 BADH family. 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-terminal sequence of pe 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, degenerated oligonucleotide 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 BADH family. 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-terminal sequence of pe (en)
Title	Pea seedling aminoaldehyde dehydrogenase: primary structure and active site residues Pea seedling aminoaldehyde dehydrogenase: primary structure and active site residues (en)
skos:prefLabel	Pea seedling aminoaldehyde dehydrogenase: primary structure and active site residues Pea seedling aminoaldehyde dehydrogenase: primary structure and active site residues (en)
skos:notation	RIV/61989592:15310/03:00001326!RIV/2004/GA0/153104/N
http://linked.open.../vavai/riv/strany	1-10
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA203/99/D048), Z(MSM 153100010)
http://linked.open...iv/cisloPeriodika	1
http://linked.open...vai/riv/dodaniDat	2004
http://linked.open...aciTvurceVysledku	Peč, Pavel Šebela, Marek
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Palackého v Olomouci / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	620510
http://linked.open...ai/riv/idVysledku	RIV/61989592:15310/03:00001326
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	BETAINE-ALDEHYDE DEHYDROGENASE, MOLECULAR-CLONING, OSMOTIC-STRESS, EXPRESSION, PLANTS, LOCALIZATION, AMARANTH, PROTEIN, GENES (en)
http://linked.open.../riv/klicoveSlovo	PROTEIN PLANTS EXPRESSION LOCALIZATION MOLECULAR-CLONING GENES AMARANTH BETAINE-ALDEHYDE DEHYDROGENASE OSMOTIC-STRESS
http://linked.open...odStatuVydavatele	FR - Francouzská republika
http://linked.open...ontrolniKodProRIV	[E520B39E4806]
http://linked.open...i/riv/nazevZdroje	Plant Physiology and Biochemistry
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (xsd:int)
http://linked.open...ocetUcastnikuAkce	0 (xsd:int)
http://linked.open...nichUcastnikuAkce	0 (xsd:int)
http://linked.open...vavai/riv/projekt	Purification of plant aminoaldehyde dehydrogenase and its enzymological characterization
http://linked.open...UplatneniVysledku	2003
http://linked.open...v/svazekPeriodika	41
http://linked.open...iv/tvurceVysledku	Snégaroff, Jacques Šebela, Marek Peč, Pavel Brauner, František Meunier, Jean-Claude
http://linked.open...n/vavai/riv/zamer	http://linked.opendata.cz/resource/domain/vavai/zamer/MSM%20153100010
issn	0981-9428
number of pages	10 (xsd:int)
http://localhost/t...ganizacniJednotka	15310

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