Quantum-chemical insight into the reaction mechanism of polypeptide UDP-GalNAc transferase 2, a retaining glycosyltransferase

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F12%3A00064681" target="_blank" >RIV/00216224:14310/12:00064681 - isvavai.cz</a>
Result on the web
<a href="http://www.xray.cz/setkani/abst2012/trnka.htm" target="_blank" >http://www.xray.cz/setkani/abst2012/trnka.htm</a>
DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Quantum-chemical insight into the reaction mechanism of polypeptide UDP-GalNAc transferase 2, a retaining glycosyltransferase
Original language description
Protein glycosylation is thought to be main means of cell recognition. Misregulation of the cascade of glycosyltransferases is related to many diseases with the most prominent example being cancer. There is thus significant scientific interest in the reaction mechanisms of glycosyltransferases. However, reaction mechanism of the configuration-retaining group of glycosyltransferases hasn't been explained yet. For his 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 protein serine or threonine hydroxyls, forming the first bond of the so-called O-linked glycosylation pathway. Increased activity of this enzyme has been found to enable metastasis of breast and colorectal cancer.
Czech name
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Czech description
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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)

Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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