MD Simulation of Glycosyltransferase LgtC in Water and in Solution of NaCl

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00010580" target="_blank" >RIV/00216224:14310/04:00010580 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
MD Simulation of Glycosyltransferase LgtC in Water and in Solution of NaCl
Original language description
The glycosyltransferases catalyze the transfer of glycosyl moieties from a donor sugar to an acceptor. These enzymes are classified as retaining or inverting, depending on the stereochemical outcome of the catalyzed reaction. An interactive database of known 3D structures of glycosyltransferases has been developed, available on http://www.cermav.cnrs.fr/cgi-bin/rxgt/rxgt.cgi. The galactosyltransferase LgtC (EC 2.4.1.44) [1, 2] from Neisseria meningitidis is a retaining glycosyltransferase catalyzing a key step in the biosynthesis of lipooligosaccharide (LOS) structure by transferring alpha-D-galactose from UDP-galactose to a terminal lactose. Elucidation of the reaction mechanism of LgtC is essential for design of enzyme inhibitors, which could be potentially used as effective antibiotics against the pathogenic bacteria Neisseria meningitidis, major cause of bacterial meningitis. First molecular dynamics (MD) simulations, performed on complex LgtC with manganese ion and donor substrate
Czech name
MD simulace na LgtC ve vodě a NaCl
Czech description
MD simulace na LgtC ve vodě a NaCl

Project
<a href="/en/project/LN00A016" target="_blank" >LN00A016: BIOMOLECULAR CENTER</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2004
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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