Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F11%3A10223645" target="_blank" >RIV/61989592:15310/11:10223645 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1111/j.1742-4658.2011.08239.x" target="_blank" >http://dx.doi.org/10.1111/j.1742-4658.2011.08239.x</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/j.1742-4658.2011.08239.x" target="_blank" >10.1111/j.1742-4658.2011.08239.x</a>

Result language
angličtina
Original language name
Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases
Original language description
The characterization of the PsAMADH2 proteins, altered here by site-directed mutagenesis, suggests that the D110 and D113 residues at the entrance to the substrate channel are required for high-affinity binding of omega-aminoaldehydes to PsAMADH2 and forenzyme activity, whereas N162, near catalytic C294, contributes mainly to the enzyme's catalytic rate. Inside the substrate cavity, W170 and Y163, and, to a certain extent, L166 and M167 probably preserve the optimal overall geometry of the substrate channel that allows for the appropriate orientation of the substrate. Unconserved W288 appears to affect the affinity of the enzyme for the substrate amino group through control of the substrate channel diameter without affecting the reaction rate. Therefore, W288 may be a key determinant of the differences in substrate specificity found among plant AMADH isoforms when they interact with naturally occurring substrates such as 3-aminopropionaldehyde and 4-aminobutyraldehyde.
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)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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