4DBC
Substrate Activation in Aspartate Aminotransferase
Summary for 4DBC
| Entry DOI | 10.2210/pdb4dbc/pdb |
| Descriptor | Aspartate aminotransferase, SULFATE ION, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | aminotransferase, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 44368.67 |
| Authors | Toney, M.D.,Fisher, A.J.,Griswold, W.R. (deposition date: 2012-01-14, release date: 2012-12-05, Last modification date: 2024-02-28) |
| Primary citation | Griswold, W.R.,Castro, J.N.,Fisher, A.J.,Toney, M.D. Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase. J.Am.Chem.Soc., 134:8436-8438, 2012 Cited by PubMed Abstract: Binding isotope effects for l-aspartate reacting with the inactive K258A mutant of PLP-dependent aspartate aminotransferase to give a stable external aldimine intermediate are reported. They provide direct evidence for electronic ground-state destabilization via hyperconjugation. The smaller equilibrium isotope effect with deazaPLP-reconstituted K258A indicates that the pyridine nitrogen plays an important role in labilizing the Cα-H bond. PubMed: 22551424DOI: 10.1021/ja302809e PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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