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.
    SYSNO ASEP0359314
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevStructural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes
    Tvůrce(i) Tylichová, M. (CZ)
    Kopečný, D. (CZ)
    Moréra, S. (FR)
    Briozzo, P. (FR)
    Lenobel, René (UEB-Q) ORCID
    Snégaroff, J. (FR)
    Šebela, M. (CZ)
    Zdroj.dok.Journal of Molecular Biology. - : Elsevier - ISSN 0022-2836
    Roč. 396, č. 4 (2010), s. 870-882
    Poč.str.13 s.
    Jazyk dok.eng - angličtina
    Země vyd.GB - Velká Británie
    Klíč. slovaaminoaldehyde dehydrogenase ; betaine aldehyde dehydrogenase ; NAD+ complex
    Vědní obor RIVCE - Biochemie
    CEPGA522/08/0555 GA ČR - Grantová agentura ČR
    GA301/08/1649 GA ČR - Grantová agentura ČR
    CEZAV0Z50380511 - UEB-Q (2005-2011)
    UT WOS000275385600005
    DOI10.1016/j.jmb.2009.12.015
    AnotaceHere, 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.
    PracovištěÚstav experimentální botaniky
    KontaktDavid Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469
    Rok sběru2011
Počet záznamů: 1  

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