Autor: Kopecny, D.; Koncitikova, R.; Tylichova, M.; Vigouroux, A.; Moskalikova, H.; Soural, M.; Sebela, M.; Morera, S.
Název práce v češtině: Rostlinné ALDH10
Název práce v angličtině: Plant ALDH10 Family
Studentská publikace: ne
Klíčová slova v češtině: aminoaldehyd dehydrogenáza, ALDH10,betain aldehyd dehydrogenáza
Klíčová slova v angličtině: aminoaldehyde dehydrogenase; ALDH10; betaine aldehyde dehydrogenase; tomato; maize
Abstrakt česky: Práce je zaměřena na studium aldehyd dehydrogenáz ALDH10
Abstrakt anglicky: Plant ALDH10 family members are aminoaldehyde dehydrogenases (AMADHs), which oxidize ω-aminoaldehydes to the corresponding acids. They have been linked to polyamine catabolism, osmoprotection, secondary metab. (fragrance), and carnitine biosynthesis. Plants commonly contain two AMADH isoenzymes. We previously studied the substrate specificity of two AMADH isoforms from peas (PsAMADHs). Here, two isoenzymes from tomato (Solanum lycopersicum), SlAMADHs, and three AMADHs from maize (Zea mays), ZmAMADHs, were kinetically investigated to obtain further clues to the catalytic mechanism and the substrate specificity. We also solved the high resoln. crystal structures of SlAMADH1 and ZmAMADH1a because these enzymes stand out from the others regarding their activity. From the structural and kinetic anal., we can state that five residues at positions 163, 288, 289, 444, and 454 (PsAMADHs numbering) can, directly or not, significantly modulate AMADH substrate specificity. In the SlAMADH1 structure, a polyethylene glycol (PEG) aldehyde derived from the precipitant PEG forms a thiohemiacetal intermediate, never obsd. so far. Its absence in the SlAMADH1-E260A structure suggests that Glu-260 can activate the catalytic cysteine as a nucleophile. We show that the five AMADHs studied here are capable of oxidizing 3-dimethylsulfoniopropionaldehyde (DMSPAL) to the cryo- and osmoprotectant 3-dimethylsulfoniopropionate (DMSP). For the first time, we also show that 3-acetamidopropionaldehyde (ACAPAL), the third aminoaldehyde besides 3-aminopropionaldehyde (APAL) and 4-aminobutyraldehyde (ABAL), is generally oxidized by AMADHs, meaning that these enzymes are unique in metabolizing and detoxifying aldehyde products of polyamine degrdn. to nontoxic amino acids. Finally, gene expression profiles in maize indicate that AMADHs might be important for controlling ω-aminoaldehyde levels during early stages of the seed development.
Jazyk v originále: angličtina
Název časopisu: J. Biological Chem.
Rok: 2013
Svazek (ročník): 288
Číslo časopisu v rámci uvedeného svazku: 13
Strana od-do: 9491-9507

Q1: ne

ISSN časopisu: 0021-9258
Vydavatel: American Society for Biochemistry and Molecular Biology.
Způsob financování: P501/11/1591, 522/08/055