4dbc | pdb_00004dbc

Substrate Activation in Aspartate Aminotransferase

spinqualitylabelsall models 4dbc, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4dbc is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3QP, EDO, SO4 Activity: Aspartate transaminase, with EC number 2.6.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 Calpha-H bond. Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase.,Griswold WR, Castro JN, Fisher AJ, Toney MD J Am Chem Soc. 2012 May 23;134(20):8436-8. doi: 10.1021/ja302809e. Epub 2012 May , 10. PMID:22551424 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate Aminotransferase

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