[50] Tryptophanase from Escherichia coli B/1t7-A
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Elsevier
Reference20 articles.
1. Application of a direct spectrophotometric assay employing a chromogenic substrate for tryptophanase to the determination of pyridoxal and pyridoxamine 5′-phosphates
2. Direct spectrophotometric assay of tryptophanase
3. The Relation of Spectral Changes and Tritium Exchange Reactions to the Mechanism of Tryptophanase-catalyzed Reactions
4. Some effects of indole on the interaction of amino acids with tryptophanase.
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1. Use of Selective Trp Side Chain Labeling To Characterize Protein−Protein and Protein−Ligand Interactions by NMR Spectroscopy;Journal of the American Chemical Society;2003-02-15
2. Pyridoxal phosphate binding to wild type, W330F, and C298S mutants ofEscherichia coliapotryptophanase: unraveling the cold inactivation;FEBS Letters;1998-08-21
3. 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
4. Tryptophanase-catalysed degradation of D-tryptophan in highly concentrated diammonium hydrogen phosphate solution;Amino Acids;1996
5. Conversion of Tryptophan, Indole-3-Pyruvic Acid, Indole-3-Lactic Acid and Indole to Indole-3-Acetic Acid by Azospirillum brasilense Sp7;Azospirillum VI and Related Microorganisms;1995
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