Reaction mechanism of retaining glycosyltransferases - a computational study

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F13%3A00072803" target="_blank" >RIV/00216224:14740/13:00072803 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Reaction mechanism of retaining glycosyltransferases - a computational study

Popis výsledku v původním jazyce

Glycosylation of cell surface proteins plays a crucial role in cell communication and recognition. Alterations in glycan structures are linked to many diseases with the most prominent example being cancer. To understand the regulation of glycosylation and to be able to modify it, reaction mechanisms of involved glycosyltransferases need to be known. However, reaction mechanism of the configuration-retaining group of glycosyltransferases hasn't been sufficiently explained yet. For this reason we have chosen a retaining glycosyltransferase ? polypeptide UDP-GalNAc transferase (ppGalNAcT) ? as the subject of our quantum-chemical study. This enzyme catalyses the transfer of N-acetylgalactosamine moiety onto serine or threonine hydroxyls, forming the firstbond of the so-called O-linked glycosylation pathway. Increased activity of ppGalNAcT has been found to enable metastasis of breast and colorectal cancer.

Název v anglickém jazyce

Reaction mechanism of retaining glycosyltransferases - a computational study

Popis výsledku anglicky

Glycosylation of cell surface proteins plays a crucial role in cell communication and recognition. Alterations in glycan structures are linked to many diseases with the most prominent example being cancer. To understand the regulation of glycosylation and to be able to modify it, reaction mechanisms of involved glycosyltransferases need to be known. However, reaction mechanism of the configuration-retaining group of glycosyltransferases hasn't been sufficiently explained yet. For this reason we have chosen a retaining glycosyltransferase ? polypeptide UDP-GalNAc transferase (ppGalNAcT) ? as the subject of our quantum-chemical study. This enzyme catalyses the transfer of N-acetylgalactosamine moiety onto serine or threonine hydroxyls, forming the firstbond of the so-called O-linked glycosylation pathway. Increased activity of ppGalNAcT has been found to enable metastasis of breast and colorectal cancer.

Druh

O - Ostatní výsledky

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

<a href="/cs/project/ED1.1.00%2F02.0068" target="_blank" >ED1.1.00/02.0068: CEITEC - central european institute of technology</a><br>

Návaznosti

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

Rok uplatnění

2013

Kód důvěrnosti údajů

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