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• W2023803631 abstract "Textbooks describe enzymes as relatively rigid templates for the transition state of a chemical reaction, and indeed an enzyme such as chymotrypsin, which catalyzes a relatively simple hydrolysis reaction, is reasonably well described by this model. Inosine monophosphate dehydrogenase (IMPDH) undergoes a remarkable array of conformational transitions in the course of a complicated catalytic cycle, offering a dramatic counterexample to this view. IMPDH displays several other unusual mechanistic features, including an Arg residue that may act as a general base catalyst and a dynamic monovalent cation site. Further, IMPDH appears to be involved in 'moon-lighting' functions that may require additional conformational states. How the balance between conformational states is maintained and how the various conformational states interconvert is only beginning to be understood." @default.
• W2023803631 created "2016-06-24" @default.
• W2023803631 creator A5062265481 @default.
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• W2023803631 date "2006-10-01" @default.
• W2023803631 modified "2023-10-17" @default.
• W2023803631 title "IMP dehydrogenase: structural schizophrenia and an unusual base" @default.
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• W2023803631 doi "https://doi.org/10.1016/j.cbpa.2006.08.005" @default.
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