Výpočetní studie na Galactosyltransferase LgtC

Kód výsledku v 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>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Computational Study of Galactosyltransferase LgtC in Complex with Manganese Ion and Donor Substrate

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

Computational Study of Galactosyltransferase LgtC in Complex with Manganese Ion and Donor Substrate

Popis výsledku anglicky

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

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2004

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název statě ve sborníku

Cukrblik 2004: Current Chemistry and Biochemistry of Saccharides

ISBN

—

ISSN

—

e-ISSN

—

Počet stran výsledku

1

Strana od-do

6-6

Název nakladatele

Ústav chemie přírodních látek VŠCHT

Místo vydání

Praha

Místo konání akce

Praha

Datum konání akce

1. 1. 2004

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

—