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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F04%3A00010189%21RIV08-MSM-14310___
rdf:type
n3:Vysledek skos:Concept
dcterms:description
The 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. Galactosyltransferase LgtC from Neisseria meningitidis has been subject to molecular dynamics simulations. Interesting differences in behavior were found for trajectories with and without donor substrate UDP-Gal. Analysis of water molecules in the active site of LgtC revealed different coordination number of manganese ion in presence and absence of the donor substrate. Stability of complex LgtC-Mn2+-UDPGal was confirmed, which is a good starting point for MD simulations of LgtC with Mn2+ ion, donor and acceptor substrates altogether. Our work is aimed at the elucidation of reaction mechanism of LgtC, which still remains a mystery. The knowledge of the reaction mechanism of this enzyme is essential for the design of effective inhibitors, which coul Výpočetní studie na Galactosyltransferase LgtC The 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. Galactosyltransferase LgtC from Neisseria meningitidis has been subject to molecular dynamics simulations. Interesting differences in behavior were found for trajectories with and without donor substrate UDP-Gal. Analysis of water molecules in the active site of LgtC revealed different coordination number of manganese ion in presence and absence of the donor substrate. Stability of complex LgtC-Mn2+-UDPGal was confirmed, which is a good starting point for MD simulations of LgtC with Mn2+ ion, donor and acceptor substrates altogether. Our work is aimed at the elucidation of reaction mechanism of LgtC, which still remains a mystery. The knowledge of the reaction mechanism of this enzyme is essential for the design of effective inhibitors, which coul
dcterms:title
Výpočetní studie na Galactosyltransferase LgtC Computational Study of Galactosyltransferase LgtC in Complex with Manganese Ion and Donor Substrate Computational Study of Galactosyltransferase LgtC in Complex with Manganese Ion and Donor Substrate
skos:prefLabel
Výpočetní studie na Galactosyltransferase LgtC Computational Study of Galactosyltransferase LgtC in Complex with Manganese Ion and Donor Substrate Computational Study of Galactosyltransferase LgtC in Complex with Manganese Ion and Donor Substrate
skos:notation
RIV/00216224:14310/04:00010189!RIV08-MSM-14310___
n4:strany
6-6
n4:aktivita
n12:P
n4:aktivity
P(LN00A016)
n4:dodaniDat
n9:2008
n4:domaciTvurceVysledku
n5:3466272 n5:1139002 n5:4347374
n4:druhVysledku
n20:D
n4:duvernostUdaju
n15:S
n4:entitaPredkladatele
n10:predkladatel
n4:idSjednocenehoVysledku
558472
n4:idVysledku
RIV/00216224:14310/04:00010189
n4:jazykVysledku
n17:eng
n4:klicovaSlova
molecular dynamics; glycosyltransferase; LgtC
n4:klicoveSlovo
n8:LgtC n8:glycosyltransferase n8:molecular%20dynamics
n4:kontrolniKodProRIV
[831ECDDFAA1C]
n4:mistoKonaniAkce
Praha
n4:mistoVydani
Praha
n4:nazevZdroje
Cukrblik 2004: Current Chemistry and Biochemistry of Saccharides
n4:obor
n18:CE
n4:pocetDomacichTvurcuVysledku
3
n4:pocetTvurcuVysledku
4
n4:projekt
n11:LN00A016
n4:rokUplatneniVysledku
n9:2004
n4:tvurceVysledku
Koča, Jaroslav Imberty, Anne Šnajdrová, Lenka Kulhánek, Petr
n4:typAkce
n6:WRD
n4:zahajeniAkce
2004-01-01+01:00
s:numberOfPages
1
n19:hasPublisher
Vysoká škola chemicko-technologická v Praze. Fakulta potravinářské a biochemické technologie. Ústav chemie přírodních látek
n14:organizacniJednotka
14310