The environments ofTrp-248 and Trp-330 in tryptophan indole-lyase fromEscherichia coli
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(90)81011-C/fullpdf
Reference27 articles.
1. The Chemical Structure of Tryptophanase from Escherichia coli
2. Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12
3. Role of cysteine residues in tryptophanase for monovalent cation-induced activation
4. The Reactivity of One Essential Cysteine as a Conformational Probe in Escherichia coli Tryptophanase. Application to the Study of the Structural Influence of Subunit Interactions
5. The interaction of Escherichia coli Tryptophanase with Various Amino Acids and Their Analogs
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1. Inhibition of Escherichia coli tryptophan indole-lyase by tryptophan homologues;Archives of Biochemistry and Biophysics;2014-10
2. Conformational changes and loose packing promote E. coli Tryptophanase cold lability;BMC Structural Biology;2009-10-08
3. 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
4. Pyridoxal phosphate binding to wild type, W330F, and C298S mutants ofEscherichia coliapotryptophanase: unraveling the cold inactivation;FEBS Letters;1998-08-21
5. Cold inactivation and dissociation into dimers of Escherichia coli tryptophanase and its W330F mutant form;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1998-05
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