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• W1993641344 abstract "Classical molecular dynamics simulations of the d-Gln/Aquifex pyrophilus MurI and d-Glu/Aquifex pyrophilus MurI complexes have been carried out. Since the active site of the enzyme contains many charged and polar residues, several binding modes are possible. Thus, three very different stable conformations of the substrate analogue d-Gln have been found, and at least three binding modes are possible for the substrate d-Glu. These qualitative results give an explanation for the apparent disagreement between the d-Gln bound MurI X-ray crystal structure and the expected position and orientation of the substrate d-Glu in order to make it possible the assumed Cα deprotonation (by Cys70)/reprotonation (by Cys178) racemization mechanism." @default.
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• W1993641344 date "2005-05-24" @default.
• W1993641344 modified "2023-10-09" @default.
• W1993641344 title "A Molecular Dynamics Simulation of the Binding Modes of <scp>d</scp>-Glutamate and <scp>d</scp>-Glutamine to Glutamate Racemase" @default.
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• W1993641344 doi "https://doi.org/10.1021/ct049881g" @default.
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• W1993641344 hasPublicationYear "2005" @default.
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