Example for the binding energy computation of phosphate ion on the surface of LDH from Lactococcus lactis type 1 Version 1
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Output files of phosphate probe binding on the surface of LDH from lactococcus lactis type 1. File with extension XPLOR can be visualized with a program VMD to identify the most favorable position for the phosphate binding. This relates to the Model "Part 4".
SEEK ID: https://fairdomhub.org/data_files/1126?version=1
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LACTIS1-GRID.tar
Format: Tar archive
Size: 52.1 MB
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Created: 7th May 2014 at 16:14
Last updated: 8th Nov 2017 at 15:21
Last used: 9th Dec 2018 at 10:33
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Projects: SysMO-LAB
Institutions: Heidelberg Institute for Theoretical Studies (HITS gGmbH), University of Heidelberg
Comparative Systems Biology: Lactic Acid Bacteria
Programme: SysMO
Public web page: http://www.sysmo.net/index.php?index=57
Challenge: Comparative analyses, as demonstrated by comparative genomics and bioinformatics, are extremely powerful for (i) transfer of information from (experimentally) well-studied organisms to the other organisms, and (ii) when coupled to functional and phenotypic information, insight in the relative importance of components to the observed differences and simalities. The central principle of this proposal is that important aspects of the functional differences between organisms derive not
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The two lactic acid bacteria L. lactis and S. pyogenes were studied with respect to the concentration of intracellular metabolites involved in glycolysis in time upon a glucose pulse. Models that describe this behavior are also constructed
Person responsible: Martijn Bekker
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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)
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Abstract:
Authors: Anna Feldman-Salit, Silvio Hering, Nadine Veith, Vlad Cojocaru, Antje Sieg, Hans Westerhoff, Bernd Kreikemeyer, Rebecca Wade, Tomas Fiedler, Messiha H.
Date Published: 17th May 2013
Journal: Journal of Biological Chemistry
