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The many faces of aspartate kinases
Authors:Dumas Renaud  Cobessi David  Robin Adeline Y  Ferrer Jean-Luc  Curien Gilles
Affiliation:CEA, iRTSV, Laboratoire de Physiologie Cellulaire et Végétale, F-38054 Grenoble, France. rdumas@cea.fr
Abstract:Based on recent X-ray structures and biochemical characterizations of aspartate kinases from different species, we show in this review how various organizations of a regulatory domain have contributed to the different mechanisms of control observed in aspartate kinases allowing simple to complex allosteric controls in branched pathways. The aim of this review is to show the relationships between domain organization, effector binding sites, mechanism of inhibition and regulatory function of an allosteric enzyme in a biosynthetic pathway.
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