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rdf:type
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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 first bond of the so-called O-linked glycosylation pathway. Increased activity of ppGalNAcT has been found to enable metastasis of breast and colorectal cancer.
- 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 first bond of the so-called O-linked glycosylation pathway. Increased activity of ppGalNAcT has been found to enable metastasis of breast and colorectal cancer. (en)
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Title
| - Reaction mechanism of retaining glycosyltransferases - a computational study
- Reaction mechanism of retaining glycosyltransferases - a computational study (en)
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skos:prefLabel
| - Reaction mechanism of retaining glycosyltransferases - a computational study
- Reaction mechanism of retaining glycosyltransferases - a computational study (en)
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skos:notation
| - RIV/00216224:14740/13:00072803!RIV14-MSM-14740___
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http://linked.open...avai/predkladatel
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/00216224:14740/13:00072803
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - retaining glycosyltransferases; reaction mechanism; density functional theory; potential energy surface (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...ontrolniKodProRIV
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...UplatneniVysledku
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http://linked.open...iv/tvurceVysledku
| - Koča, Jaroslav
- Kozmon, Stanislav
- Trnka, Tomáš
- Tvaroška, Igor
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http://localhost/t...ganizacniJednotka
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