Site-directed Mutagenesis of Residues at Subunit Interfaces of Porcine Fructose-1,6-bisphosphatase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference38 articles.
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2. 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
3. Crystal Structures of Human Muscle Fructose-1,6-Bisphosphatase: Novel Quaternary States, Enhanced AMP Affinity, and Allosteric Signal Transmission Pathway;PLoS ONE;2013-09-27
4. Mechanism of Displacement of a Catalytically Essential Loop from the Active Site of Mammalian Fructose-1,6-bisphosphatase;Biochemistry;2013-07-24
5. Roles of the Residues Lys115 and Tyr116 in the Binding of an Allosteric Inhibitor AMP to Pea Cytosolic Fructose-1,6-bisphosphatase;Journal of Applied Biological Chemistry;2008-04-30
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