"GAP501/11/1591" . "Structure-functional characterization of selected plant aldehyde dehydrogenases"@en . . "http://www.isvav.cz/projectDetail.do?rowId=GAP501/11/1591"^^ . . . . . . . . . "0"^^ . . . . . . "The project provided new, so far unknown information about the function of some specific plant enzymes and several enzymes related to biosynthesis of aldehydes. The defined aims were met. The results were published in five journals with a higher impact factor. They enable further development of the problem and are important for teaching. No shortcomings were found."@en . "Strukturn\u011B-funk\u010Dn\u00ED charakterizace vybran\u00FDch rostlinn\u00FDch aldehyddehydrogenas" . "1"^^ . "aldehyde dehydrogenase maize (Zea mays) antiquitin site-directed mutagenesis"@en . . . "2013-06-07+02:00"^^ . "0"^^ . . "Aldehydes appear as intermediates in various biochemical pathways but they are usually highly reactive and toxic at higher levels. Aldehyde dehydrogenases (ALDHs) have been considered as general detoxifying enzymes which eliminate biogenic and xenobiotic aldehydes in an NAD(P)+-dependent manner. There are twelve ALDH families in plants. We are going to perform a comparative study on substrate specificity of eleven plant enzymes from maize (Zea mays), which cover five ALDH families, followed by structure-functional and gene expression studies. Our strategy involves gene cloning, expression, biochemical characterization of recombinant proteins, elucidation of the catalysis and mapping of active-site residues involved in the substrate recognition (supported by experiments of site-directed mutagenesis). Several enzymes will be crystallized and their protein structures solved by X-ray diffraction. The obtained results will allow us to understand physiological roles of the respective ALDHs and provide data for their possible application in biotechnology and bioanalytical approaches."@en . "2014-07-01+02:00"^^ . "5"^^ . "2011-01-01+01:00"^^ . . "5"^^ . "Projekt p\u0159inesl nov\u00E9, dosud nezn\u00E1m\u00E9 informace o funkci n\u011Bkolika specifick\u00FDch rostlinn\u00FDch enzym\u016F a n\u011Bkolika enzym\u016F spojen\u00FDch s biosynt\u00E9zou aldehyd\u016F. Stanoven\u00E9 c\u00EDle byly napln\u011Bny. V\u00FDsledky byly publikov\u00E1ny v 5 \u010Dasopisech s vy\u0161\u0161\u00EDm impaktem. V\u00FDsledky umo\u017E\u0148uj\u00ED dal\u0161\u00ED rozvoj problematiky a jsou v\u00FDznamn\u00E9 z hlediska v\u00FDuky. Nedostatky nebyly zji\u0161t\u011Bny."@cs . "2013-12-31+01:00"^^ . . "Aldehydy se objevuj\u00ED jako meziprodukty v\u00A0r\u016Fzn\u00FDch biochemick\u00FDch drah\u00E1ch, ale p\u0159i vy\u0161\u0161\u00EDch hladin\u00E1ch jsou obvykle vysoce reaktivn\u00ED a toxick\u00E9. Aldehyddehydogenasy (ALDH) jsou pova\u017Eov\u00E1ny za v\u0161eobecn\u011B detoxika\u010Dn\u00ED enzymy, kter\u00E9 odstra\u0148uj\u00ED biogenn\u00ED a cizorod\u00E9 aldehydy NAD(P)+-dependentn\u00EDm zp\u016Fsobem. V\u00A0rostlin\u00E1ch existuje dvan\u00E1ct ALDH rodin. Provedeme srovn\u00E1vac\u00ED studii substr\u00E1tov\u00E9 specifi\u010Dnosti jeden\u00E1cti rostlinn\u00FDch enzym\u016F z kuku\u0159ice (Zea mays), kter\u00E9 p\u0159\u00EDslu\u0161\u00ED k p\u011Bti ALDH rodin\u00E1m, a n\u00E1sledn\u011B studii strukturn\u011B-funk\u010Dn\u00ED a studii genov\u00E9 exprese. Na\u0161e strategie zahrnuje klonov\u00E1n\u00ED gen\u016F, expresi, biochemickou charakterizaci rekombinantn\u00EDch protein\u016F, objasn\u011Bn\u00ED katal\u00FDzy a mapov\u00E1n\u00ED rezidu\u00ED v\u00A0aktivn\u00EDm m\u00EDst\u011B zapojen\u00FDch do rozpozn\u00E1n\u00ED substr\u00E1tu (podpo\u0159en\u00E9 experimenty m\u00EDstn\u011B-\u0159\u00EDzen\u00E9 mutageneze). N\u011Bkolik enzym\u016F bude krystalizov\u00E1no a jejich proteinov\u00E9 struktury \u0159e\u0161eny rentgeno-strukturn\u00ED anal\u00FDzou. Z\u00EDskan\u00E9 v\u00FDsledky n\u00E1m umo\u017En\u00ED pochopit fyziologick\u00E9 \u00FAlohy jednotliv\u00FDch ALDH a poskytnou \u00FAdaje pro jejich mo\u017En\u00E9 pou\u017Eit\u00ED v oblasti biotechnologi\u00ED a bioanalytick\u00FDch p\u0159\u00EDstup\u016F." . .