Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 519, Issue 2, Pages 186-193Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2011.10.016
Keywords
Aspartate kinase; ACT domain; Control; Allostery; Structure; Metabolism
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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. (C) 2011 Elsevier Inc. All rights reserved.
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