Structural Models and Binding Studies of Epsilon-Trimethyllysine Hydroxylase

Riga Technical University 57th International Scientific Conference "Materials Science and Applied Chemistry" (MSAC 2016) : Proceedings and Programme 2016
Diāna Zeļencova-Gopejenko, Edvards Liepiņš

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.

Keywords
ε-Trimethyllysine Hydroxylase (TMLH), Molecular Dynamics (MD), Ligand Docking, Nuclear Magnetic Resonance (NMR).
Hyperlink
https://conferences.rtu.lv/index.php/MSAC/MSAC2016/paper/viewFile/42/22

Zeļencova, D., Liepiņš, E. Structural Models and Binding Studies of Epsilon-Trimethyllysine Hydroxylase. In: Riga Technical University 57th International Scientific Conference "Materials Science and Applied Chemistry" (MSAC 2016) : Proceedings and Programme, Latvia, Riga, 21-21 October, 2016. Riga: RTU Press, 2016, pp.196-200. ISBN 978-9934-10-861-7.

Publication language
English (en)