Truncated Forms of the Recombinant Escherichia coli ADP-Glucose Pyrophosphorylase: The Importance of the N-Terminal Region for Allosteric Activation and Inhibition

By Wu M-X.   Preiss J.  

Archives of Biochemistry and Biophysics, Vol. 389, Iss. 2, 2001-05 ,pp. : 159-165

Elsevier

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The N-terminal Domain of the Regulatory Subunit is Sufficient for Complete Activation of Acetohydroxyacid Synthase III from Escherichia coli

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Academic Press

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Characterization of ADP-Glucose Pyrophosphorylase from Rhodobacter sphaeroides 2.4.1: Evidence for the Involvement of Arginine in Allosteric Regulation

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Archives of Biochemistry and Biophysics, Vol. 372, Iss. 1, 1999-12 ,pp. : 179-188

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A Kinetic Study of Site-Directed Mutants of Escherichia coli ADP-Glucose Pyrophosphorylase: The Role of Residue 295 in Allosteric Regulation

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Site-Directed Mutagenesis of a Regulatory Site of Escherichia coli ADP-Glucose Pyrophosphorylase: The Role of Residue 336 in Allosteric Behavior

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