Plant ALDH10 family: identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F13%3A33147799" target="_blank" >RIV/61989592:15310/13:33147799 - isvavai.cz</a>
Result on the web
<a href="http://www.jbc.org/content/288/13/9491" target="_blank" >http://www.jbc.org/content/288/13/9491</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/jbc.M112.443952" target="_blank" >10.1074/jbc.M112.443952</a>

Result language
angličtina
Original language name
Plant ALDH10 family: identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate
Original language description
Plant ALDH10 family members are aminoaldehyde dehydrogenases (AMADHs), which oxidize omega-aminoaldehydes to the corresponding acids. They have been linked to polyamine catabolism, osmoprotection, secondary metabolism (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 resolution crystal structures of SlAMADH1 and ZmAMADH1a because these enzymes stand out from the others regarding their activity. From the structural and kinetic analysis, 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 SlA
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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