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

0359314 - ÚEB 2011 RIV GB eng J - Journal Article
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. E-ISSN 1089-8638
R&D Projects: GA ČR GA522/08/0555; GA ČR GA301/08/1649
Institutional research plan: CEZ:AV0Z50380511
Keywords : aminoaldehyde dehydrogenase * betaine aldehyde dehydrogenase * NAD+ complex
Subject RIV: CE - Biochemistry
Impact factor: 4.008, year: 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.
Permanent Link: http://hdl.handle.net/11104/0197118