Exploring the Evolution of Novel Enzyme Functions within Structurally Defined Protein Superfamilies

Nicholas Furnham, Ian Sillitoe, Gemma L. Holliday, Alison L. Cuff, Roman A. Laskowski, Christine A. Orengo, Janet M. Thornton, Yanay Ofran
<span title="2012-03-01">2012</span> <i title="Public Library of Science (PLoS)"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/ch57atmlprauhhbqdf7x4ytejm" style="color: black;">PLoS Computational Biology</a> </i> &nbsp;
scale motions that are quenched upon PPACK binding. TROSY Hahn-echo and relaxation dispersion experiments reveal a large number of residues throughout the protein undergoing temporally correlated ms-ms motions. These include the Na þ -binding loop and the b-strand connecting exosite 1 and the active site, both of which are implicated in allosteric coupling of effector binding sites with the active site. The results show a network of slowly exchanging residues extends through the entire
more &raquo; ... bin molecule. 164-Symp Enzyme activity is essential for almost all aspects of life. With completely sequenced genomes, the full complement of enzymes in an organism can be defined, and 3D structures have been determined for many enzyme families. Traditionally each enzyme has been studied individually, but as more enzymes are characterised it is now timely to revisit the molecular basis of catalysis, by comparing different enzymes and their mechanisms, and to consider how complex pathways and networks may have evolved. New approaches to understanding enzymes mechanisms and how enzyme families evolve functional diversity will be described. 1.Martinez Cuesta S, Furnham N, Rahman SA, Sillitoe I, Thornton JM. The evolution of enzyme function in the isomerases.
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