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Publikācija: Structural Models and Binding Studies of Epsilon-Trimethyllysine Hydroxylase

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Nosaukums oriģinālvalodā Structural Models and Binding Studies of Epsilon-Trimethyllysine Hydroxylase
Pētniecības nozare 1. Dabaszinātnes
Pētniecības apakšnozare 1.4. Ķīmija
Autori Diāna Zeļencova
Edvards Liepiņš
Atslēgas vārdi ε-Trimethyllysine Hydroxylase (TMLH), Molecular Dynamics (MD), Ligand Docking, Nuclear Magnetic Resonance (NMR).
Anotācija ε-Trimethyllysine Hydroxylase (TMLH) is a new target enzyme which modulates the energetic processes in the organism by regulation the level of bioavailable carnitine. TMLH is the first enzyme in carnitine biosynthesis. Its inhibition is proposed to have more potent cardioprotective effect than meldonium that inhibits the last step of the carnitine formation. The study is devoted to the design and evaluation of three-dimensional structure of TMLH in silico, accompanied with protein-ligand binding studies in silico and in vitro. The possible enzyme active site and ligand binding modes were predicted and supported with the NMR experimental data.
Hipersaite: https://conferences.rtu.lv/index.php/MSAC/MSAC2016/paper/viewFile/42/22 
Atsauce Zeļencova, D., Liepiņš, E. Structural Models and Binding Studies of Epsilon-Trimethyllysine Hydroxylase. No: Riga Technical University 57th International Scientific Conference "Materials Science and Applied Chemistry" (MSAC 2016) : Proceedings and Programme, Latvija, Riga, 21.-21. oktobris, 2016. Riga: RTU Press, 2016, 196.-200.lpp. ISBN 978-9934-10-861-7.
ID 24101