Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase

Benzer Materyaller

• The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure.
  Yazar:: Baker, D. P., ve diğerleri
  Baskı/Yayın Bilgisi: (1996)
• Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase
  Yazar:: Fetler, Luc, ve diğerleri
  Baskı/Yayın Bilgisi: (2007)
• Asymmetric Allosteric Signaling in Aspartate Transcarbamoylase
  Yazar:: Mendes, Kimberly R., ve diğerleri
  Baskı/Yayın Bilgisi: (2010)
• Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylase.
  Yazar:: Baker, D. P., ve diğerleri
  Baskı/Yayın Bilgisi: (1995)
• Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure.
  Yazar:: Tauc, P., ve diğerleri
  Baskı/Yayın Bilgisi: (1994)