TAILIEUCHUNG - Báo cáo khoa học: Kinetic mechanism for p38 MAP kinase a A partial rapid-equilibrium random-order ternary-complex mechanism for the phosphorylation of a protein substrate

p38 Mitogen-activated protein kinase alpha (p38 MAPKa) is a member of the MAPK family. It is activated by cellular stresses and has a number of cellular substrates whose coordinated regulation mediates inflammatory responses. In addition, it is a useful anti-inflammatory drug target that has a high specificity for Ser-Pro or Thr-Pro motifs in proteins and contains a number of transcription factors as well as protein kinases in its catalog of known substrates. | FEBS Journal Kinetic mechanism for p38 MAP kinase a A partial rapid-equilibrium random-order ternary-complex mechanism for the phosphorylation of a protein substrate Anna E. Szafranska1 and Kevin N. Dalby1 2 1 Division of MedicinalChemistry University of Texas at Austin TX USA 2 Graduate Programs in Biochemistry and Molecular Biology and the Center for Molecular and Cellular Toxicology University of Texas at Austin TX USA Keywords docking inhibition kinetic mechanism MAP kinase p38 MAPK Correspondence K. N. Dalby Division of Medicinal Chemistry College of Pharmacy University of Texas at Austin TX 78712 USA Fax 1 512 232 2606 Tel 1 512 471 9267 E-mail Dalby@ Received 28 February 2005 revised 18 May 2005 accepted 20 June 2005 doi p38 Mitogen-activated protein kinase alpha p38 MAPKa is a member of the MAPK family. It is activated by cellular stresses and has a number of cellular substrates whose coordinated regulation mediates inflammatory responses. In addition it is a useful anti-inflammatory drug target that has a high specificity for Ser-Pro or Thr-Pro motifs in proteins and contains a number of transcription factors as well as protein kinases in its catalog of known substrates. Fundamental to signal transduction research is the understanding of the kinetic mechanisms of protein kinases and other protein modifying enzymes. To achieve this end because peptides often make only a subset of the full range of interactions made by proteins protein substrates must be utilized to fully elucidate kinetic mechanisms. We show using an untagged highly active form of p38 MAPKa expressed and purified from Escherichia coli Szafranska AE Luo X Dalby KN 2005 Anal Biochem 336 1-10 that at pH 10 mm Mg2 and 27 C p38 MAPKa phosphorylates ATF2A115 through a partial rapid-equilibrium randomorder ternary-complex mechanism. This mechanism is supported by a combination of steady-state substrate and inhibition kinetics as well as .

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