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Mechanistic characterization for c-jun-n-terminal kinase 1 alpha 1

Academic Article
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Overview

authors

  • Ember, B.
  • LoGrasso, Philip

publication date

  • September 2008

journal

  • Archives of Biochemistry and Biophysics  Journal

abstract

  • c-jun-N-terminal kinase 1alpha1 (JNK1alpha1) is a serine/threonine kinase of the mitogen-activated protein (MAP) kinase family that phosphorylates protein transcription factors after activation by a variety of environmental stressors. In this study, the kinetic mechanism for JNK1alpha1 phosphorylation of activating transcription factor 2 (ATF2) was determined utilizing steady-state kinetics in the presence and absence of both ATF2 and ATP competitive inhibitors. Data from initial velocity studies were consistent with a sequential mechanism for JNK1alpha1. AMP-PCP exhibited competitive inhibition versus ATP and pure noncompetitive inhibition versus ATF2. JIP-1 peptide (RPKRPTTLNLF) was competitive versus ATF2 and mixed noncompetitive versus ATP. These data suggest that JNK1alpha1 proceeded via a random sequential kinetic mechanism with non-interacting ATF2 and ATP substrate sites.

subject areas

  • Activating Transcription Factor 2
  • Adaptor Proteins, Signal Transducing
  • Adenosine Triphosphate
  • Computer Simulation
  • Enzyme Activation
  • Mitogen-Activated Protein Kinase 8
  • Models, Chemical
  • Peptide Fragments
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Research

keywords

  • ATF2
  • JIP
  • JNK
  • MAP kinase
  • c-jun
  • kinetic mechanism
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Identity

International Standard Serial Number (ISSN)

  • 0003-9861

Digital Object Identifier (DOI)

  • 10.1016/j.abb.2008.06.001

PubMed ID

  • 18559253
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Additional Document Info

start page

  • 324

end page

  • 329

volume

  • 477

issue

  • 2

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