Linkage between Fructose 1,6-Bisphosphate Binding and the Dimer−Tetramer Equilibrium of Escherichia coli Glycerol Kinase: Critical Behavior Arising from Change of Ligand Stoichiometry-Reference-Cited by-同舟云学术

Linkage between Fructose 1,6-Bisphosphate Binding and the Dimer−Tetramer Equilibrium of Escherichia coli Glycerol Kinase: Critical Behavior Arising from Change of Ligand Stoichiometry

Published:2003-03-20 Issue:14 Volume:42 Page:4243-4252
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Yu Peng¹,Pettigrew Donald W.¹

Affiliation:

1. Department of Biochemistry and Biophysics, Center for Advanced Biomolecular Research, Texas A&M University, College Station, Texas 77843-2128

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi027142l

Reference35 articles.

1. Production of an activated form of Bacillus stearothermophilus L-2-hydroxyacid dehydrogenase by directed evolution

2. An absolute requirement of fructose 1,6-bisphosphate for the Lactobacillus caseil-lactate dehydrogenase activity induced by a single amino acid substitution

3. Molecular Basis of Allosteric Activation of Bacterial l-Lactate Dehydrogenase

4. Mutations that significantly change the stability, flexibility and quaternary structure of the l-lactate dehydrogenase from Bacillus megaterium

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