Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 10, Issue 5, Pages 520-525Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2006.08.005
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- NIGMS NIH HHS [GM54403] Funding Source: Medline
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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.
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