"Ornithin-delta-aminotransferasa (OAT) je mitochondri\u00E1ln\u00ED enzym obsahuj\u00EDc\u00ED pyridoxal-5\u00B4-fosf\u00E1t, kter\u00FD katalyzuje p\u0159em\u011Bnu L-ornithinu na L-glutam\u00E1t-\u03B3-semialdehyd s pou\u017Eit\u00EDm 2-oxoglutar\u00E1tu jako koncov\u00E9ho akceptoru aminoskupiny. Byl pops\u00E1n v \u0159ad\u011B organism\u016F. Na z\u00E1klad\u011B krystalov\u00E9 struktury lidsk\u00E9 OAT je velmi dob\u0159e prouzkoum\u00E1n princip vazby substr\u00E1tu a reak\u010Dn\u00ED mechanismus enzymu. OAT m\u00E1 vlastnosti velmi podobn\u00E9 ostatn\u00EDm enzym\u016Fm z podskupiny 3 aminotransferas. V rostlin\u00E1ch se enzym \u00FA\u010Dastn\u00ED biosynt\u00E9zy a akumulace prolinu, co\u017E je jedna z cest regulace osmolarity v odpov\u011Bdi na osmotick\u00FD stres."@cs . . . "ornithine delta-aminotransferase; osmotic stress; proline; \u03941-pyrroline-5-carboxylate; pyridoxal-5'-phosphate; semialdehyde; transamination"@en . "1559-2316" . "\u0160ebela, Marek" . . "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 \u03B3-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 . "RIV/61989592:15310/08:00005308!RIV09-MSM-15310___" . "Plant Signalling & Behavior" . . "11" . "US - Spojen\u00E9 st\u00E1ty americk\u00E9" . . "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 \u03B3-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" . "Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants" . "3" . . "Sn\u00E9garoff, Jacques" . . "[FCE51B103F81]" . "Ornithin-delta-aminotransferasa: enzym zapojen\u00FD do mechanism\u016F salinitn\u00ED tolerance u vy\u0161\u0161\u00EDch rostlin"@cs . . "RIV/61989592:15310/08:00005308" . . . . "Kope\u010Dn\u00FD, David" . "7"^^ . . "Str\u00E1nsk\u00E1, Jana" . "1"^^ . "Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants" . . "Tylichov\u00E1, Martina" . . "15310" . . "Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants"@en . . . . . "Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants"@en . "385393" . "Ornithin-delta-aminotransferasa: enzym zapojen\u00FD do mechanism\u016F salinitn\u00ED tolerance u vy\u0161\u0161\u00EDch rostlin"@cs . "P(GA522/08/0555), P(GD522/08/H003), S" . . "5"^^ . .