About: Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Ornithine-delta-aminotransferase (OAT, EC 2.6.1.13) catalyzes the transamination of L-ornithine to L-glutamate-gamma-semialdehyde. We investigated the enzyme from pea (PsOAT). First, a cDNA coding for PsOAT was cloned and expressed in Escherichia coli. Recombinant PsOAT was purified under native conditions and its molecular and kinetic properties were characterized. The purified PsOAT existed asa monomer of 50 kDa and showed typical spectral properties of enzymes containing pyridoxal-5?-phosphate as a prosthetic group. L-Ornithine was the best substrate but PsOAT also slowly converted N(alpha)-acetyl-L-ornithine. In these reactions, 2-oxoglutarate was the exclusive amino group acceptor. The enzyme had a basic optimal pH of 8.8 anddisplayed relatively high temperature optimum. Diamines and polyamines were not accepted assubstrates. On the other hand, putrescine, spermidine and others represented weak non-competitive inhibitors. Ornithine-delta-aminotransferase (OAT, EC 2.6.1.13) catalyzes the transamination of L-ornithine to L-glutamate-gamma-semialdehyde. We investigated the enzyme from pea (PsOAT). First, a cDNA coding for PsOAT was cloned and expressed in Escherichia coli. Recombinant PsOAT was purified under native conditions and its molecular and kinetic properties were characterized. The purified PsOAT existed asa monomer of 50 kDa and showed typical spectral properties of enzymes containing pyridoxal-5?-phosphate as a prosthetic group. L-Ornithine was the best substrate but PsOAT also slowly converted N(alpha)-acetyl-L-ornithine. In these reactions, 2-oxoglutarate was the exclusive amino group acceptor. The enzyme had a basic optimal pH of 8.8 anddisplayed relatively high temperature optimum. Diamines and polyamines were not accepted assubstrates. On the other hand, putrescine, spermidine and others represented weak non-competitive inhibitors. (en)
Title	Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines (en)
skos:prefLabel	Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines (en)
skos:notation	RIV/61989592:15110/10:10212789!RIV11-GA0-15110___
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(GA522/08/0555), P(GD522/08/H003)
http://linked.open...iv/cisloPeriodika	8
http://linked.open...vai/riv/dodaniDat	2011
http://linked.open...aciTvurceVysledku	STRÁNSKÁ, Jana
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 / Lékařská fakulta
http://linked.open...dnocenehoVysledku	248828
http://linked.open...ai/riv/idVysledku	RIV/61989592:15110/10:10212789
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	pyridoxal-5'-phosphate; proline; polyamine; ornithine-delta-aminotransferase; ornithine (en)
http://linked.open.../riv/klicoveSlovo	proline ornithine ornithine-delta-aminotransferase polyamine pyridoxal-5'-phosphate
http://linked.open...odStatuVydavatele	FR - Francouzská republika
http://linked.open...ontrolniKodProRIV	[C1AEEF428C01]
http://linked.open...i/riv/nazevZdroje	Biochimie
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (xsd:int)
http://linked.open...vavai/riv/projekt	Integration of doctoral studies in biochemistry, plant physiology and biophysics Structure-functional characterization of oxidoreductases acting on nitrogenous regulatory compounds in plants
http://linked.open...UplatneniVysledku	2010
http://linked.open...v/svazekPeriodika	92
http://linked.open...iv/tvurceVysledku	STRÁNSKÁ, Jana KOPEČNÝ, David TYLICHOVÁ, Martina ŠEBELA, Marek SNÉGAROFF, Jacques
http://linked.open...ain/vavai/riv/wos	000280570800004
issn	0300-9084
number of pages	9 (xsd:int)
http://localhost/t...ganizacniJednotka	15110
is http://linked.open...avai/riv/vysledek of	Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines

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