Communication between Thiamin Cofactors in the Escherichia coli Pyruvate Dehydrogenase Complex E1 Component Active Centers: EVIDENCE FOR A “DIRECT PATHWAY” BETWEEN THE 4′-AMINOPYRIMIDINE N1′ ATOMS

Documenti analoghi

• Novel Binding Motif and New Flexibility Revealed by Structural Analyses of a Pyruvate Dehydrogenase-Dihydrolipoyl Acetyltransferase Subcomplex from the Escherichia coli Pyruvate Dehydrogenase Multienzyme Complex
  di: Arjunan, Palaniappa, et al.
  Pubblicazione: (2014)
• Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex
  di: Wang, Junjie, et al.
  Pubblicazione: (2014)
• Bifunctionality of the thiamin diphosphate cofactor: assignment of tautomeric/ionization states of the 4′-aminopyrimidine ring when various intermediates occupy the active sites during the catalysis of yeast pyruvate decarboxylase
  di: Balakrishnan, Anand, et al.
  Pubblicazione: (2012)
• Multiple roles of mobile active center loops in the E1 component of the Escherichia coli pyruvate dehydrogenase complex - Linkage of protein dynamics to catalysis
  di: Jordan, Frank, et al.
  Pubblicazione: (2009)
• Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural Approaches
  di: Chandrasekhar, Krishnamoorthy, et al.
  Pubblicazione: (2013)