A Chimeric Bacterial Phosphofructokinase Exhibits Cooperativity in the Absence of Heterotropic Regulation
Open Access
- 1 February 1995
- journal article
- Published by Elsevier
- Vol. 270 (8) , 3828-3835
- https://doi.org/10.1074/jbc.270.8.3828
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction productsPublished by Elsevier ,2005
- Kinetic Characteristics of Phosphofructokinase from Bacillus stearothermophilus: MgATP Nonallosterically Inhibits the EnzymeBiochemistry, 1994
- Substrate antagonism in the kinetic mechanism of E. coli phosphofructokinase‐1FEBS Letters, 1991
- pH dependence of the kinetic properties of allosteric phosphofructokinase from Escherichia coliBiochemistry, 1991
- Fructose‐6‐phosphate modifies the pathway of the urea‐induced dissociation of the allosteric phosphofructokinase from Escherichia coliFEBS Letters, 1990
- Active-site mutants altering the cooperativity of E. coliphosphofructokinaseNature, 1990
- Structural basis of the allosteric behaviour of phosphofructokinaseNature, 1990
- Dissection of the effector-binding site and complementation studies of Escherichia coli phosphofructokinase using site-directed mutagenesisBiochemistry, 1989
- Nucleotide sequence and high‐level expression of the major Escherichia coli phosphofructokinaseEuropean Journal of Biochemistry, 1985
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970