Role and structural characterization of plant aldehyde dehydrogenases from family 2 and family 7
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
25734422
DOI
10.1042/bj20150009
PII: BJ20150009
Knihovny.cz E-zdroje
- MeSH
- aldehyddehydrogenasa chemie genetika metabolismus MeSH
- fylogeneze MeSH
- hrách setý enzymologie genetika MeSH
- izoenzymy chemie genetika metabolismus MeSH
- katalytická doména genetika MeSH
- kinetika MeSH
- krystalografie rentgenová MeSH
- kukuřice setá enzymologie genetika MeSH
- modely genetické MeSH
- molekulární modely MeSH
- molekulární sekvence - údaje MeSH
- NAD metabolismus MeSH
- rostlinné proteiny chemie genetika metabolismus MeSH
- rostliny enzymologie genetika MeSH
- sekvence aminokyselin MeSH
- stanovení celkové genové exprese MeSH
- substrátová specifita MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aldehyddehydrogenasa MeSH
- izoenzymy MeSH
- NAD MeSH
- rostlinné proteiny MeSH
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 α-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 cell wall 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.
Citace poskytuje Crossref.org
GENBANK
KJ004509, KJ004510, KJ004511, KJ004512, KJ004513, KM225857, KM225858
PDB
4PXL, 4PXN, 4PZ2