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Review
. 2012 Mar 15;519(2):186-93.
doi: 10.1016/j.abb.2011.10.016. Epub 2011 Nov 6.

The many faces of aspartate kinases

Renaud Dumas  1 , David Cobessi, Adeline Y Robin, Jean-Luc Ferrer, Gilles Curien
Affiliations
Review

The many faces of aspartate kinases

Renaud Dumas et al. Arch Biochem Biophys. .

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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