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Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes
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SYSNO ASEP 0359314 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes Author(s) Tylichová, M. (CZ)
Kopečný, D. (CZ)
Moréra, S. (FR)
Briozzo, P. (FR)
Lenobel, René (UEB-Q) ORCID
Snégaroff, J. (FR)
Šebela, M. (CZ)Source Title Journal of Molecular Biology. - : Elsevier - ISSN 0022-2836
Roč. 396, č. 4 (2010), s. 870-882Number of pages 13 s. Language eng - English Country GB - United Kingdom Keywords aminoaldehyde dehydrogenase ; betaine aldehyde dehydrogenase ; NAD+ complex Subject RIV CE - Biochemistry R&D Projects GA522/08/0555 GA ČR - Czech Science Foundation (CSF) GA301/08/1649 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z50380511 - UEB-Q (2005-2011) UT WOS 000275385600005 DOI 10.1016/j.jmb.2009.12.015 Annotation 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. Workplace Institute of Experimental Botany Contact David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Year of Publishing 2011
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