Computational Study of Galactosyltransferase LgtC in Complex with Manganese Ion and Donor Substrate
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00010189" target="_blank" >RIV/00216224:14310/04:00010189 - 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
Computational Study of Galactosyltransferase LgtC in Complex with Manganese Ion and Donor Substrate
Original language 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, donorand 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 inhibi
Czech name
Výpočetní studie na Galactosyltransferase LgtC
Czech description
Výpočetní studie na Galactosyltransferase 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
Cukrblik 2004: Current Chemistry and Biochemistry of Saccharides
ISBN
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ISSN
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e-ISSN
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Number of pages
1
Pages from-to
6-6
Publisher name
Ústav chemie přírodních látek VŠCHT
Place of publication
Praha
Event location
Praha
Event date
Jan 1, 2004
Type of event by nationality
WRD - Celosvětová akce
UT code for WoS article
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