Directed Mutations in the Poorly Defined Region of Porcine Liver Fructose-1,6-bisphosphatase Significantly Affect Catalysis and the Mechanism of AMP Inhibition
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference36 articles.
1. Interaction of fructose 2,6-bisphosphate and AMP with fructose-1,6-bisphosphatase as studied by nuclear magnetic resonance spectroscopy.
2. The Allosteric Properties of Beef-Liver Fructose Bisphosphatase
3. Inhibition of fructose-1,6-bisphosphatase by fructose 2,6-biphosphate.
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1. Central Cavity of Fructose-1,6-bisphosphatase and the Evolution of AMP/Fructose 2,6-bisphosphate Synergism in Eukaryotic Organisms;Journal of Biological Chemistry;2014-03
2. Ligand-based designing, in silico screening, and biological evaluation of new potent fructose-1,6-bisphosphatase (FBPase) inhibitors;European Journal of Medicinal Chemistry;2012-10
3. Structures of Mammalian and Bacterial Fructose-1,6-bisphosphatase Reveal the Basis for Synergism in AMP/Fructose 2,6-Bisphosphate Inhibition;Journal of Biological Chemistry;2007-12
4. Expression of key substrate cycle enzymes in rat spermatogenic cells: Fructose 1,6 bisphosphatase and 6 phosphofructose 1-kinase;Journal of Cellular Physiology;2007
5. Origin of Cooperativity in the Activation of Fructose-1,6-bisphosphatase by Mg2+;Journal of Biological Chemistry;2004-04
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