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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. (cs)
  • 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 (en)
Title
  • Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants
  • Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants (en)
  • Ornithin-delta-aminotransferasa: enzym zapojený do mechanismů salinitní tolerance u vyšších rostlin (cs)
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 (en)
  • Ornithin-delta-aminotransferasa: enzym zapojený do mechanismů salinitní tolerance u vyšších rostlin (cs)
skos:notation
  • RIV/61989592:15310/08:00005308!RIV09-MSM-15310___
http://linked.open...avai/riv/aktivita
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  • P(GA522/08/0555), P(GD522/08/H003), S
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  • 11
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  • 385393
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  • RIV/61989592:15310/08:00005308
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  • ornithine delta-aminotransferase; osmotic stress; proline; Δ1-pyrroline-5-carboxylate; pyridoxal-5'-phosphate; semialdehyde; transamination (en)
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  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [FCE51B103F81]
http://linked.open...i/riv/nazevZdroje
  • Plant Signalling & Behavior
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http://linked.open...v/svazekPeriodika
  • 3
http://linked.open...iv/tvurceVysledku
  • Kopečný, David
  • Snégaroff, Jacques
  • Tylichová, Martina
  • Šebela, Marek
  • Stránská, Jana
issn
  • 1559-2316
number of pages
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  • 15310
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