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Detail publikace

Autor: Frömmel, J.; Soural, M.; Tylichová, M.; Kopečný, D.; Demo G.; Wimmerová, M.; Šebela, M.
Název práce v češtině: Rostlinné aminoaldehyd-dehydrogenázy oxidují široké spektrum dusíkatých heterocyklických aldehydů
Název práce v angličtině: Plant aminoaldehyde dehydrogenases oxidize a wide range of nitrogenous heterocyclic aldehydes
Studentská publikace: ne

Klíčová slova v angličtině: aldehyde, aminoaldehyde, dehydrogase, purine, pyrimidine, pyridine
Abstrakt česky: Metabolická degradace enzymů je katalyzovaná oxidoreduktázami, z nichž aldehyddehydrogenázy představují nespecifické, resp. substrátově specifické enzymy. Článek popisuje kinetickou studii substrátové specifity isoenzymů z rajčete a hrachu proti škále aldehydů obsahujících dusíkatý skelet na bázi purinu, deazapurinu, pyrimidinu a pyridinu.
Abstrakt anglicky: The metabolic degradation of aldehydes is catalyzed by oxidoreductases from which aldehydedehydrogenases (EC 1.2.1) comprise nonspecific or substrate-specific enzymes. The latter subset isrepresented e.g. by NAD+-dependent aminoaldehyde dehydrogenases (AMADHs; EC 1.2.1.19)oxidizing a group of naturally occurring ω-aminoaldehydes including polyamine oxidation products.Recombinant isoenzymes from pea (PsAMADH1 and 2) and tomato (LeAMADH1 and 2) weresubjected to kinetic measurements with synthetic aldehydes containing a nitrogenous heterocycle suchas pyridinecarbaldehydes and their halogenated derivatives, (pyridinylmethylamino)-aldehydes,pyridinyl propanals and aldehydes derived from purine, 7-deazapurine and pyrimidine to characterizetheir substrate specificity and significance of the resulting data for in vivo reactions. The enzymaticproduction of the corresponding carboxylic acids was analyzed by liquid chromatography coupled toelectrospray ionization mass spectrometry. Although the studied AMADHs are largely homologousand supposed to have a very similar active site architecture, significant differences were observed.LeAMADH1 displayed the broadest specificity oxidizing almost all compounds followed byPsAMADH2 and 1. In contrast, LeAMADH2 accepted only a few compounds as substrates. Pyridinylpropanals were converted by all isoenzymes, usually better than pyridinecarbaldehydes and aldehydeswith fused rings. The Km values for the best substrates were in the range of 10-5 to 10-4 M.Nevertheless, the catalytic efficiency values (Vmax/Km) reached only a very small fraction of that with3-aminopropanal (except for LeAMADH1 activity with two pyridine-derived compounds). Dockingexperiments using the crystal structure of PsAMADH2 were involved to discuss differ““
Jazyk v originále: angličtina
Název časopisu: Amino Acids
Rok: 2012
Svazek (ročník): 43
Číslo časopisu v rámci uvedeného svazku: 3
Strana od-do: 1189-1202

Q1: ne

Způsob financování: ED0007/01/01, 522/08/0555