Phosphorus 31 nuclear magnetic resonance study of tryptophanase. Pyridoxal phosphate-binding site.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. Formation and Interrelationships of Tryptophanase and Tryptophan Synthetases in Escherichia coli
2. Properties of Crystalline Tryptophanase
3. Reversibility of the Tryptophanase Reaction: Synthesis of Tryptophan from Indole, Pyruvate, and Ammonia
4. CATALYTIC PROPERTIES OF TRYPTOPHANASE, A MULTIFUNCTIONAL PYRIDOXAL PHOSPHATE ENZYME
5. The Subunit Structure of Tryptophanase
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1. 31P NMR spectroscopy senses the microenvironment of the 5′-phosphate group of enzyme-bound pyridoxal 5′-phosphate;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2011-11
2. Ionization state of pyridoxal 5′-phosphate in d-serine dehydratase, dialkylglycine decarboxylase and tyrosine phenol-lyase and the influence of monovalent cations as inferred by 31P NMR spectroscopy;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2006-02
3. Crystal structure of tryptophanase;Journal of Molecular Biology;1998-02
4. [4] Nuclear magnetic resonance in study of active sites of pyridoxal-dependent enzymes;Methods in Enzymology;1997
5. Equilibria and absorption spectra of tryptophanase;Journal of Biological Chemistry;1991-05
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