MD simulace na LgtC ve vodě a NaCl

Kód výsledku v 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>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2004

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název statě ve sborníku

GlycoT 2004

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

117-117

Název nakladatele

University of Lille, France

Místo vydání

Le Touquet, France

Místo konání akce

Le Touquet, France

Datum konání akce

4. 11. 2004

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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