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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F08%3A00005308%21RIV09-MSM-15310___
rdf:type
n10:Vysledek skos:Concept
dcterms:description
Ornithin-delta-aminotransferasa (OAT) je mitochondriální enzym obsahující pyridoxal-5´-fosfát, který katalyzuje přeměnu L-ornithinu na L-glutamát-γ-semialdehyd s použitím 2-oxoglutarátu jako koncového akceptoru aminoskupiny. Byl popsán v řadě organismů. Na základě krystalové struktury lidské OAT je velmi dobře prouzkoumán princip vazby substrátu a reakční mechanismus enzymu. OAT má vlastnosti velmi podobné ostatním enzymům z podskupiny 3 aminotransferas. V rostlinách se enzym účastní biosyntézy a akumulace prolinu, což je jedna z cest regulace osmolarity v odpovědi na osmotický stres. This review deals with biochemical and physiological aspects of plant ornithine delta-aminotransferase (OAT, EC 2.6.1.13). OAT is a mitochondrial enzyme containing pyridoxal-5'-phosphate as a cofactor, which catalyzes the conversion of L-ornithine to L-glutamate γ-semialdehyde using 2-oxoglutarate as a terminal amino group acceptor. It has been described in humans, animals, insects, plants and microorganisms. Based on the crystal structure of human OAT, both substrate binding and reaction mechanism of the enzyme are well understood. OAT shows a large structural and mechanistic similarity to other enzymes from the subgroup III of aminotransferases, which transfer an amino group from a carbon atom that does not carry a carboxyl function. In plants, the enzyme has been implicated in proline biosynthesis and accumulation (via pyrroline-5-carboxylate), which represents a way to regulate cellular osmolarity in response to osmotic stress. However, the exact metabolic pathway involving OAT remains This review deals with biochemical and physiological aspects of plant ornithine delta-aminotransferase (OAT, EC 2.6.1.13). OAT is a mitochondrial enzyme containing pyridoxal-5'-phosphate as a cofactor, which catalyzes the conversion of L-ornithine to L-glutamate γ-semialdehyde using 2-oxoglutarate as a terminal amino group acceptor. It has been described in humans, animals, insects, plants and microorganisms. Based on the crystal structure of human OAT, both substrate binding and reaction mechanism of the enzyme are well understood. OAT shows a large structural and mechanistic similarity to other enzymes from the subgroup III of aminotransferases, which transfer an amino group from a carbon atom that does not carry a carboxyl function. In plants, the enzyme has been implicated in proline biosynthesis and accumulation (via pyrroline-5-carboxylate), which represents a way to regulate cellular osmolarity in response to osmotic stress. However, the exact metabolic pathway involving OAT remains
dcterms:title
Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants Ornithin-delta-aminotransferasa: enzym zapojený do mechanismů salinitní tolerance u vyšších rostlin Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants
skos:prefLabel
Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants Ornithin-delta-aminotransferasa: enzym zapojený do mechanismů salinitní tolerance u vyšších rostlin
skos:notation
RIV/61989592:15310/08:00005308!RIV09-MSM-15310___
n4:aktivita
n15:S n15:P
n4:aktivity
P(GA522/08/0555), P(GD522/08/H003), S
n4:cisloPeriodika
11
n4:dodaniDat
n6:2009
n4:domaciTvurceVysledku
n17:9708790
n4:druhVysledku
n13:J
n4:duvernostUdaju
n12:S
n4:entitaPredkladatele
n14:predkladatel
n4:idSjednocenehoVysledku
385393
n4:idVysledku
RIV/61989592:15310/08:00005308
n4:jazykVysledku
n5:eng
n4:klicovaSlova
ornithine delta-aminotransferase; osmotic stress; proline; Δ1-pyrroline-5-carboxylate; pyridoxal-5'-phosphate; semialdehyde; transamination
n4:klicoveSlovo
n9:pyridoxal-5%27-phosphate n9:semialdehyde n9:osmotic%20stress n9:transamination n9:ornithine%20delta-aminotransferase n9:%CE%941-pyrroline-5-carboxylate n9:proline
n4:kodStatuVydavatele
US - Spojené státy americké
n4:kontrolniKodProRIV
[FCE51B103F81]
n4:nazevZdroje
Plant Signalling & Behavior
n4:obor
n18:CE
n4:pocetDomacichTvurcuVysledku
1
n4:pocetTvurcuVysledku
5
n4:projekt
n11:GD522%2F08%2FH003 n11:GA522%2F08%2F0555
n4:rokUplatneniVysledku
n6:2008
n4:svazekPeriodika
3
n4:tvurceVysledku
Šebela, Marek Snégaroff, Jacques Kopečný, David Stránská, Jana Tylichová, Martina
s:issn
1559-2316
s:numberOfPages
7
n16:organizacniJednotka
15310