Reaction mechanism of retaining glycosyltransferases - a computational study
The result's identifiers
Result code in 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>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Reaction mechanism of retaining glycosyltransferases - a computational study
Original language description
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.
Czech name
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Czech description
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Classification
Type
O - Miscellaneous
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/ED1.1.00%2F02.0068" target="_blank" >ED1.1.00/02.0068: Central european institute of technology</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů