Conformational dynamics of the enzyme-substrate complex of protein kinase A with pseudosubstrate SP20 and adenosine triphosphate
Mulashkina T.I.1 , Leonova M.S.2, Khrenova M.G.3
1. Chemistry Department, Lomonosov Moscow State University, Moscow, Russia 2. Chemistry Department, Lomonosov Moscow State University, Moscow, Russia; Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, Moscow, Russia 3. Chemistry Department, Lomonosov Moscow State University, Moscow, Russia; Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences, Moscow, Russia
The phosphorylation reaction, catalyzed by the enzyme protein kinase A (PKA), plays one of the key roles in the work of the glutamatergic system, primarily involved in memory functioning. The analysis of the dynamic behavior of the enzyme-substrate complex allows one to learn the mechanism of the enzymatic reaction. According to the results of classical molecular dynamics calculations followed by hierarchical clustering, the most preferred proton acceptor during the phosphorylation reaction catalyzed by PKA is the carboxyl group of the amino acid residue Asp166; however, the γ-phosphate group of ATP can also act as an acceptor.
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Keywords: protein kinase A, molecular dynamics, conformations, enzyme-substrate complex, ATP
Citation:
Mulashkina T.I., Leonova M.S., Khrenova M.G. (2024) Conformational dynamics of the enzyme-substrate complex of protein kinase A with pseudosubstrate SP20 and adenosine triphosphate. Biomeditsinskaya Khimiya, 70(6), 421-427.
Mulashkina T.I. et al. Conformational dynamics of the enzyme-substrate complex of protein kinase A with pseudosubstrate SP20 and adenosine triphosphate // Biomeditsinskaya Khimiya. - 2024. - V. 70. -N 6. - P. 421-427.
Mulashkina T.I. et al., "Conformational dynamics of the enzyme-substrate complex of protein kinase A with pseudosubstrate SP20 and adenosine triphosphate." Biomeditsinskaya Khimiya 70.6 (2024): 421-427.
Mulashkina, T. I., Leonova, M. S., Khrenova, M. G. (2024). Conformational dynamics of the enzyme-substrate complex of protein kinase A with pseudosubstrate SP20 and adenosine triphosphate. Biomeditsinskaya Khimiya, 70(6), 421-427.
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