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Regulation of the activity of lactate dehydrogenases from four lactic acid bacteria

SysMO-LAB

Despite high similarity in sequence and catalytic properties, the L-lactate dehydrogenases (LDH) in lactic acid bacteria (LAB) display differences in their regulation which may arise from their adaptation to different habitats. We combined experimental and computational approaches to investigate the effects of fructose-1,6-bisphosphate (FBP), phosphate (Pi) and ionic strength (NaCl concentration) on 6 LDHs from 4 LABs studied at pH 6 and pH 7. We find: (1) The extent of activation by FBP (Kact) ...

Submitter: Anna Feldman-Salit

Biological problem addressed: Metabolism

Investigation: Investigation of glycolysis and pyruvate branch...

Study: Comparative modeling and phosphate dependence f...

Organisms: Lactococcus lactis, Streptococcus pyogenes, Enterococcus faecalis, Lactobacillus plantarum

Models: Part 1: Comparative modeling of 3D structures o..., Part 2: Computation of electrostatic potentials..., Part 3: Comparison of electrostatic potentials ..., Part 4: Activation / Inhibition Effect on LDHs ..., Part 5: Algorithm to computationally estimate t...

SOPs: No SOPs

Data files: 3D-sturctures of Lactate Dehydrogenase from 4 L..., Activation / Inhibition of 4 LDH enzymes in the..., Comparison of electrostatic potentials of LDH e..., Electrostatic potentials of four LDH enzymes fr..., Example for the binding energy computation of p..., Measurements on kinetics of L-LDHs from differe..., The effects of fructose-1,6-bisphosphate, phosp...

Snapshots: No snapshots

Created: 19th Feb 2014 at 13:08, Last updated: 8th Nov 2017 at 14:21

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