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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Kreikemeyer, Bernd Westerhoff, Hans V. Sieg, Antje Veith, Nadine Cojocaru, Vlad Fiedler, Tomas Feldman-salit, Anna Wade, Rebecca C. Messiha, Hanan L. Hering, Silvio |
| Description | Author Affiliation: Feldman-Salit A ( Molecular and Cellular Modeling Group, Heidelberg Institute for Theoretical Studies, 69118 Heidelberg, Germany.) |
| Abstract | Despite high similarity in sequence and catalytic properties, the l-lactate dehydrogenases (LDHs) in lactic acid bacteria (LAB) display differences in their regulation that 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 six LDHs from four LABs studied at pH 6 and pH 7. We found that 1) the extent of activation by FBP (Kact) differs. Lactobacillus plantarum LDH is not regulated by FBP, but the other LDHs are activated with increasing sensitivity in the following order: Enterococcus faecalis LDH2 ≤ Lactococcus lactis LDH2 < E. faecalis LDH1 < L. lactis LDH1 ≤ Streptococcus pyogenes LDH. This trend reflects the electrostatic properties in the allosteric binding site of the LDH enzymes. 2) For L. plantarum, S. pyogenes, and E. faecalis, the effects of Pi are distinguishable from the effect of changing ionic strength by adding NaCl. 3) Addition of Pi inhibits E. faecalis LDH2, whereas in the absence of FBP, Pi is an activator of S. pyogenes LDH, E. faecalis LDH1, and L. lactis LDH1 and LDH2 at pH 6. These effects can be interpreted by considering the computed binding affinities of Pi to the catalytic and allosteric binding sites of the enzymes modeled in protonation states corresponding to pH 6 and pH 7. Overall, the results show a subtle interplay among the effects of Pi, FBP, and pH that results in different regulatory effects on the LDHs of different LABs. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 29 |
| Volume Number | 288 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2013-07-19 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bacteria Enzymology Lactate Dehydrogenases Metabolism Lactic Acid Allosteric Regulation Drug Effects Binding Sites Biocatalysis Crystallography, X-Ray Enzyme Activation Fructosediphosphates Pharmacology Hydrogen-Ion Concentration Isoenzymes Kinetics Chemistry Isolation & Purification Models, Biological Phosphates Sodium Chloride Static Electricity Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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