Unique Kinase Catalytic Mechanism of AceK with a Single Magnesium Ion
作者： Quanjie Li , Jimin Zheng , Hongwei Tan , Xichen Li , Guangju Chen
DOI: 10.1371/JOURNAL.PONE.0072048
关键词: Plasma protein binding 、 Adenosine triphosphate 、 Transition state 、 Stereochemistry 、 Active site 、 Protein phosphorylation 、 Phosphorylation 、 Phosphatase 、 Magnesium ion 、 Chemistry 、 Biochemistry 、 General Biochemistry, Genetics and Molecular Biology 、 General Agricultural and Biological Sciences 、 General Medicine
摘要: Isocitrate dehydrogenase kinase/phosphatase (AceK) is the founding member of protein phosphorylation system in prokaryotes. Based on novel and unique structural characteristics AceK recently uncovered, we sought to understand its kinase reaction mechanism, along with other features involved phosphotransfer process. Herein report density functional theory QM calculations mechanism catalysed by AceK. The transition states located indicate that reaction, AceK, follows a dissociative Asp457 serving as catalytic base accept proton delivered substrate. Our results also revealed prefers single Mg2+-containing active site reaction. roles conserved residues are discussed.
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M. Garnak, H.C. Reeves, Purification and properties of phosphorylated isocitrate dehydrogenase of Escherichia coli. Journal of Biological Chemistry. ,vol. 254, pp. 7915- 7920 ,(1979) , 10.1016/S0021-9258(18)36033-2
S. R. Hubbard, Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. The EMBO Journal. ,vol. 16, pp. 5572- 5581 ,(1997) , 10.1093/EMBOJ/16.18.5572
Axel D. Becke, A New Mixing of Hartree-Fock and Local Density-Functional Theories Journal of Chemical Physics. ,vol. 98, pp. 1372- 1377 ,(1993) , 10.1063/1.464304
Pawel Szarek, Edyta Dyguda-Kazimierowicz, Akitomo Tachibana, W. Andrzej Sokalski, Physical nature of intermolecular interactions within cAMP-dependent protein kinase active site: differential transition state stabilization in phosphoryl transfer reaction. Journal of Physical Chemistry B. ,vol. 112, pp. 11819- 11826 ,(2008) , 10.1021/JP8040633
Natalia Díaz, Martin J. Field, Insights into the phosphoryl-transfer mechanism of cAMP-dependent protein kinase from quantum chemical calculations and molecular dynamics simulations. Journal of the American Chemical Society. ,vol. 126, pp. 529- 542 ,(2004) , 10.1021/JA037277U
M Garnak, HC Reeves, Phosphorylation of Isocitrate dehydrogenase of Escherichia coli Science. ,vol. 203, pp. 1111- 1112 ,(1979) , 10.1126/SCIENCE.34215
Jason C. Hart, Ian H. Hillier, Neil A. Burton, David W. Sheppard, AN ALTERNATIVE ROLE FOR THE CONSERVED ASP RESIDUE IN PHOSPHORYL TRANSFER REACTIONS Journal of the American Chemical Society. ,vol. 120, pp. 13535- 13536 ,(1998) , 10.1021/JA982632F
Susan Serota Taylor, Elzbieta Radzio-Andzelm, Three protein kinase structures define a common motif. Structure. ,vol. 2, pp. 345- 355 ,(1994) , 10.1016/S0969-2126(00)00036-8
Jianhua Zheng, Daniel R. Knighton, Lynn F. Ten Eyck, Rolf Karlsson, N. Xuong, Susan S. Taylor, Janusz M. Sowadski, Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry. ,vol. 32, pp. 2154- 2161 ,(1993) , 10.1021/BI00060A005
S. Hanks, A. Quinn, T Hunter, The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science. ,vol. 241, pp. 42- 52 ,(1988) , 10.1126/SCIENCE.3291115