Phosphorus-31 nuclear magnetic resonance study on cytoplasmic aspartate aminotransferase from pig heart
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference12 articles.
1. 31P Nuclear-Magnetic-Resonance Studies of Pyridoxal and Pyridoxamine Phosphates. Interaction with Cytoplasmic Aspartate Transaminase
2. 31P nuclear magnetic resonance of mitochondrial aspartate aminotransferase. The effects of solution pH and ligand binding.
3. The three-dimensional structure of mitochondrial aspartate aminotransferase at 4.5 Å resolution
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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. NMR Studies of Coupled Low- and High-Barrier Hydrogen Bonds in Pyridoxal-5‘-phosphate Model Systems in Polar Solution;Journal of the American Chemical Society;2007-04-25
3. 15N Nuclear Magnetic Resonance Studies of Acid−Base Properties of Pyridoxal-5‘-Phosphate Aldimines in Aqueous Solution;The Journal of Physical Chemistry B;2007-03-23
4. 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
5. Binding of C5-Dicarboxylic Substrate to Aspartate Aminotransferase: Implications for the Conformational Change at the Transaldimination Step,;Biochemistry;2005-05-17
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