Počet záznamů: 1

Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes

  1. 1.
    0359314 - UEB-Q 2011 RIV GB eng J - Článek v odborném periodiku
    Tylichová, M. - Kopečný, D. - Moréra, S. - Briozzo, P. - Lenobel, René - Snégaroff, J. - Šebela, M.
    Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes.
    Journal of Molecular Biology. Roč. 396, č. 4 (2010), s. 870-882 ISSN 0022-2836
    Grant CEP: GA ČR GA522/08/0555; GA ČR GA301/08/1649
    Výzkumný záměr: CEZ:AV0Z50380511
    Klíčová slova: aminoaldehyde dehydrogenase * betaine aldehyde dehydrogenase * NAD+ complex
    Kód oboru RIV: CE - Biochemie
    Impakt faktor: 4.008, rok: 2010

    Here, we report the first X-ray structures of plant AMADHs: two isoenzymes, PsAMADH1 and PsAMADH2, from Pisum sativum in complex with β-nicotinamide adenine dinucleotide (NAD+) at 2.4 and 2.15 Å resolution, respectively. Both recombinant proteins are dimeric. Each subunit binds NAD+ as a coenzyme, contains a solvent-accessible C-terminal peroxisomal targeting signal (type 1) and a cation bound in the cavity close to the NAD+ binding site. Structural analysis and substrate specificity study of both isoenzymes in combination with data published previously on other ALDH9 family members show that the established categorization of such enzymes into distinct groups based on substrate specificity is no more appropriate, because many of them seem capable of oxidizing a large spectrum of aminoaldehyde substrates. PsAMADH1 and PsAMADH2 can oxidize N,N,N-trimethyl-4-aminobutyraldehyde into γ-butyrobetaine, which is the carnitine precursor in animal cells.
    Trvalý link: http://hdl.handle.net/11104/0197118