Pyridoxal phosphate binding to wild type, W330F, and C298S mutants ofEscherichia coliapotryptophanase: unraveling the cold inactivation
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(98)00931-4/fullpdf
Reference18 articles.
1. Yu.M. Torchinsky Ya. Kawata T. Fukui K. Soda Molecular Aspects of Enzyme Catalysis 1994 VCH, Weinheim Kodansha, Tokyo 165 190
2. Equilibria and absorption spectra of tryptophanase
3. Interactions of Escherichia coli tryptophanase with quasisubstrates and monovalent cations studied by the circular dichroism and fluorescence methods
4. Kinetic and equilibrium studies on the activation of Escherichia coli K12 tryptophanase by pyridoxal 5'-phosphate and monovalent cations.
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1. A structural view of the dissociation ofEscherichia colitryptophanase;Acta Crystallographica Section D Biological Crystallography;2015-11-26
2. Conformational changes and loose packing promote E. coli Tryptophanase cold lability;BMC Structural Biology;2009-10-08
3. The mechanism of addition of pyridoxal 5′-phosphate to Escherichia coli apo-serine hydroxymethyltransferase;Biochemical Journal;2007-05-29
4. Role of Lysine-256 in Citrobacter freundii Tyrosine Phenol-lyase in Monovalent Cation Activation;Biochemistry;2004-10-19
5. Cold-induced enzyme inactivation: how does cooling lead to pyridoxal phosphate–aldimine bond cleavage in tryptophanase?;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2002-02
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