title: The many faces of aspartate kinases.
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.
authors.affiliation: CEA, iRTSV, Laboratoire de Physiologie Cellulaire et Végétale, F-38054 Grenoble, France. rdumas@cea.fr
authors.forename: Renaud
authors.initials: R
authors.lastname: Dumas
authors.forename: David
authors.initials: D
authors.lastname: Cobessi
authors.forename: Adeline Y
authors.initials: AY
authors.lastname: Robin
authors.forename: Jean-Luc
authors.initials: JL
authors.lastname: Ferrer
authors.forename: Gilles
authors.initials: G
authors.lastname: Curien
mesh_terms: D000494:Allosteric Regulation; D001222:Aspartate Kinase / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D007700:Kinetics; D017434:Protein Structure, Tertiary
chemical_list: D001222:Aspartate Kinase