MgATP-Dependent Activation by Phosphoenolpyruvate of the E187A Mutant of Escherichia coli Phosphofructokinase
Author:
Affiliation:
1. Division of Pathology and Laboratory Medicine, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030, and Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi001769r
Reference30 articles.
1. The role of Glu187 in the regulation of phosphofructokinase by phosphoenolpyruvate
2. Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products
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1. Structure of the Apo Form of Bacillus stearothermophilus Phosphofructokinase;Biochemistry;2012-01-11
2. Quantification of Allosteric Influence of Escherichia coli Phosphofructokinase by Frequency Domain Fluorescence;Biophysical Journal;2003-07
3. Creation of an Allosteric Phosphofructokinase Starting with a Nonallosteric Enzyme;Journal of Biological Chemistry;2002-01
4. Pre-steady State Quantification of the Allosteric Influence ofEscherichia coli Phosphofructokinase;Journal of Biological Chemistry;2001-09
5. Persistent Binding of MgADP to the E187A Mutant of Escherichia coli Phosphofructokinase in the Absence of Allosteric Effects;Biochemistry;2001-03-07
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