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

…, D Kopečný, S Moréra, P Briozzo, R Lenobel…

Index: Tylichova, Martina; Kopecny, David; Morera, Solange; Briozzo, Pierre; Lenobel, Rene; Snegaroff, Jacques; Sebela, Marek Journal of Molecular Biology, 2010 , vol. 396, # 4 p. 870 - 882

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Citation Number: 32

Abstract

Aminoaldehyde dehydrogenases (AMADHs, EC 1.2. 1.19) belong to the large aldehyde dehydrogenase (ALDH) superfamily, namely, the ALDH9 family. They oxidize polyamine- derived ω-aminoaldehydes to the corresponding ω-amino acids. 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 ...