Involvement of the conserved histidine-188 residue in the L-lactate dehydrogenase from thermus caldophilus GK24 in allosteric regulation by fructose 1,6-bisphosphate
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference30 articles.
1. Heat-Stable and Fructose 1,6-Bisphosphate-Activated L-Lactate Dehydrogenase from an Extremely Thermophilic Bacterium1
2. l-Lactate dehydrogenase from Thermus caldophilus GK24, an extremely thermophilic bacterium. Desensitization to fructose 1,6-bisphosphate in the activated state by arginine-specific chemical modification and the N-terminal amino acid sequence
3. Fructose 1,6-Bisphosphate-Dependent L-Lactate Dehydrogenase from Thermus aquaticus YT-1, an Extreme Thermophile: Activation by Citrate and Modification Reagents and Comparison with Thermus caldophilus GK24 L-Lactate Dehydrogenase
4. Allosteric effect of fructose 1,6-bisphosphate on the conformation of NAD+ as bound to L-lactate dehydrogenase from Thermus caldophilus GK24.
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1. Deciphering Evolutionary Trajectories of Lactate Dehydrogenases Provides New Insights into Allostery;Molecular Biology and Evolution;2023-10
2. Protein Conformational Space at the Edge of Allostery: Turning a Nonallosteric Malate Dehydrogenase into an “Allosterized” Enzyme Using Evolution-Guided Punctual Mutations;Molecular Biology and Evolution;2022-09-01
3. Modified catalytic performance of Lactobacillus fermentum l-lactate dehydrogenase by rational design;Systems Microbiology and Biomanufacturing;2021-11-20
4. Biochemical, structural and dynamical studies reveal strong differences in the thermal-dependent allosteric behavior of two extremophilic lactate dehydrogenases;Journal of Structural Biology;2021-09
5. The Core of Allosteric Motion in Thermus caldophilus l-Lactate Dehydrogenase;Journal of Biological Chemistry;2014-11
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