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rdf:type
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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
- 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)
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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)
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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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skos:notation
| - RIV/00216224:14310/04:00010189!RIV08-MSM-14310___
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http://linked.open.../vavai/riv/strany
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/00216224:14310/04:00010189
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - molecular dynamics; glycosyltransferase; LgtC (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...ontrolniKodProRIV
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http://linked.open...v/mistoKonaniAkce
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http://linked.open...i/riv/mistoVydani
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http://linked.open...i/riv/nazevZdroje
| - Cukrblik 2004: Current Chemistry and Biochemistry of Saccharides
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...UplatneniVysledku
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http://linked.open...iv/tvurceVysledku
| - Imberty, Anne
- Koča, Jaroslav
- Kulhánek, Petr
- Šnajdrová, Lenka
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http://linked.open...vavai/riv/typAkce
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http://linked.open.../riv/zahajeniAkce
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number of pages
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http://purl.org/ne...btex#hasPublisher
| - Vysoká škola chemicko-technologická v Praze. Fakulta potravinářské a biochemické technologie. Ústav chemie přírodních látek
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http://localhost/t...ganizacniJednotka
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