Number of the records: 1
Role and structural characterization of plant aldehyde dehydrogenases from family 2 and family 7
- 1.0446876 - ÚEB 2016 RIV GB eng J - Journal Article
Končitíková, R. - Vigouroux, A. - Kopečná, M. - Andree, T. - Bartoš, Jan - Šebela, M. - Moréra, S. - Kopečný, D.
Role and structural characterization of plant aldehyde dehydrogenases from family 2 and family 7.
Biochemical Journal. Roč. 468, Part: 1 (2015), s. 109-123. ISSN 0264-6021
R&D Projects: GA ČR GA15-22322S; GA MŠk(CZ) LO1204
Institutional support: RVO:61389030
Keywords : aldehyde dehydrogenase 2 (ALDH2) * aldehyde dehydrogenase 7 (ALDH7) * benzaldehyde
Subject RIV: EB - Genetics ; Molecular Biology
Impact factor: 3.562, year: 2015
Aldehyde dehydrogenases (ALDHs) are responsible for oxidation of biogenic aldehyde intermediates as well as for cell detoxification of aldehydes generated during lipid peroxidation. So far, 13 ALDH families have been described in plants. In the present study, we provide a detailed biochemical characterization of plant ALDH2 and ALDH7 families by analysing maize and pea ALDH7 (ZmALDH7 and PsALDH7) and four maize cytosolic ALDH(cALDH) 2 isoforms RF2C, RF2D, RF2E and RF2F [the first maize ALDH2 was discovered as a fertility restorer (RF2A)]. We report the crystal structures of ZmALDH7, RF2C and RF2F at high resolution. The ZmALDH7 structure shows that the three conserved residues Glu(120), Arg(300) and Thr(302) in the ALDH7 family are located in the substrate-binding site and are specific to this family. Our kinetic analysis demonstrates that alpha-aminoadipic semialdehyde, a lysine catabolism intermediate, is the preferred substrate for plant ALDH7. In contrast, aromatic aldehydes including benzaldehyde, anisaldehyde, cinnamaldehyde, coniferaldehyde and sinapaldehyde are the best substrates for cALDH2. In line with these results, the crystal structures of RF2C and RF2F reveal that their substrate-binding sites are similar and are formed by an aromatic cluster mainly composed of phenylalanine residues and several nonpolar residues. Gene expression studies indicate that the RF2C gene, which is strongly expressed in all organs, appears essential, suggesting that the crucial role of the enzyme would certainly be linked to the cellwall formation using aldehydes from phenylpropanoid pathway as substrates. Finally, plant ALDH7 may significantly contribute to osmoprotection because it oxidizes several aminoaldehydes leading to products known as osmolytes.
Permanent Link: http://hdl.handle.net/11104/0248826
File Download Size Commentary Version Access 2015_Koncitikova_BIOCHEMICAL JOURNAL_109.pdf 2 1.5 MB Other open-access
Number of the records: 1