Molecular Dynamics Simulations on Glycosyltrasferase LgtC
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00010190" target="_blank" >RIV/00216224:14310/04:00010190 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Molecular Dynamics Simulations on Glycosyltrasferase LgtC
Original language description
glycosyltransferases catalyze the transfer of glycosyl moieties from a donor sugar to an acceptor. In most cases, the donor is a nucleoside phosphosugar and the acceptor a hydroxyl group of another sugar, a lipid, or another component of glycoconjugates.The catalytic mechanism of the glycosyltransferases, however, still remains a mystery. The glycosyltransferases are classified as either retaining or inverting, depending on the stereochemical outcome of the reaction catalyzed. The galactosyltransferaseLgtC from Neisseria meningitidis is a retaning glycosyltransferase catalyzing a key step in the biosynthesis of lipooligosaccharide structure by transferring alpha-D-galactose from UDP-galactose to a terminal lactose. The comprehension of the catalyticmechanism is an essential precondition to be able to design an effective inhibitor of this enzyme, and to find an effective drug against the bacterial pathogen in this way. We report here the first molecular dynamics simulations of LgtC i
Czech name
MD simulace na LgtC
Czech description
MD simulace na LgtC
Classification
Type
D - Article in proceedings
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
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)
Others
Publication year
2004
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Article name in the collection
Materials Structure in Chemistry
ISBN
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ISSN
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e-ISSN
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Number of pages
1
Pages from-to
52-52
Publisher name
Czech and Slovak Crystallographic Association
Place of publication
Praha
Event location
Praha
Event date
Jan 1, 2004
Type of event by nationality
CST - Celostátní akce
UT code for WoS article
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