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

By Meyer C.R.   Yirsa J.   Gott B.   Preiss J.  

Archives of Biochemistry and Biophysics, Vol. 352, Iss. 2, 1998-04 ,pp. : 247-254

Elsevier

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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

By Meyer C.R.   Bork J.A.   Nadler S.   Yirsa J.   Preiss J.  

Archives of Biochemistry and Biophysics, Vol. 353, Iss. 1, 1998-05 ,pp. : 152-159

Elsevier

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The N-Terminal Region Is Important for the Allosteric Activation and Inhibition of the Escherichia coli ADP-Glucose Pyrophosphorylase

By Wu M-X.   Preiss J.  

Archives of Biochemistry and Biophysics, Vol. 358, Iss. 1, 1998-10 ,pp. : 182-188

Elsevier

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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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Investigation of Subunit Function in ADP-Glucose Pyrophosphorylase

By Kavakli I.H.   Greene T.W.   Salamone P.R.   Choi S-B.   Okita T.W.  

Biochemical and Biophysical Research Communications, Vol. 281, Iss. 3, 2001-03 ,pp. : 783-787

Elsevier

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