About: Computational Study of Galactosyltransferase LgtC in Complex with Manganese Ion and Donor Substrate     Goto   Sponge   NotDistinct   Permalink

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  • 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
  • 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 (en)
  • Výpočetní studie na Galactosyltransferase LgtC (cs)
Title
  • Výpočetní studie na Galactosyltransferase LgtC (cs)
  • 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 (en)
skos:prefLabel
  • Výpočetní studie na Galactosyltransferase LgtC (cs)
  • 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 (en)
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  • RIV/00216224:14310/04:00010189!RIV08-MSM-14310___
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  • 6-6
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  • P(LN00A016)
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  • 558472
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  • RIV/00216224:14310/04:00010189
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  • molecular dynamics; glycosyltransferase; LgtC (en)
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  • [831ECDDFAA1C]
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  • Praha
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  • Praha
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  • Cukrblik 2004: Current Chemistry and Biochemistry of Saccharides
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  • Imberty, Anne
  • Koča, Jaroslav
  • Kulhánek, Petr
  • Šnajdrová, Lenka
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  • Vysoká škola chemicko-technologická v Praze. Fakulta potravinářské a biochemické technologie. Ústav chemie přírodních látek
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