| Title: | PURIFICATION AND BIOCHEMICAL CHARACTERIZATION OF BACTERIAL GLYCOSYLTRANSFERASE |
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| Authors: | ID Kokot, Deja (Author)
ID Potočnik, Uroš (Mentor) More about this mentor...  |
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| Files: |  UNI_Kokot_Deja_2012.pdf (5,12 MB)
MD5: DD6FC4587D95F2690F3E17EF4B6E5105
PID: 20.500.12556/dkum/796011c9-0c3c-44ca-9884-4c267daccdf6
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| Language: | English |
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| Work type: | Undergraduate thesis |
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| Typology: | 2.11 - Undergraduate Thesis |
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| Organization: | FKKT - Faculty of Chemistry and Chemical Engineering
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| Abstract: | It has been estimated that over half of all proteins found in nature are glycosylated, with more than three quarters of these containing N-linked carbohydrates. N-Glycosylation, one of the most common and yet complex forms of post-translational modification, is involved in many cellular processes including protein folding, protein secretion, intracellular trafficking and cell communication.
Sialic acids form diverse family of negatively charged sugars that play essential biological roles. Their synthesis is regulated by large set of enzymes. Sialyltransferases are key enzymes for the biosynthesis of sialic acid-containing molecules, which have been implicated in various biological and phatological processes including cell-cell recognition, cell growth and differentiation, cancer metastasis, immunological regulation, as well as bacterial and viral infection. They transfere sialic acid residue, usually from an activated sugar nucleotide donor cytidine 5'monophosphate sialic acid (CMP-Sia) to a suitable acceptor to formation of a sialyl linkage with high stereo and regio-selectivity. Several eukaryotic and bacterial sialyltransferases have been described up to date. All eukaryotic sialyltransferases are grouped into a single glycosyltransferase family GT29 based on their sequence similarities. However on the other hand, bacterial sialyltransferases indentified up to date have been grouped into four glycosyltransferase families including GT38, GT42, GT52 and GT80.
The aim of this work was the indentification, purification, expression and biochemical characterization of a new member of GT80 family sialyltransferase from Pasteurella dagmatis.
In this work we describe a new bacterial sialyltransferase beta-galactoside alpha-2,3-sialyltransferase, a bacterial sialyltransferase obtained from Pasteurella dagmatis and a member of a GT80 family based on its sequence similarity. It is multifunctional enzyme which has four major activities including α2,3-sialyltransferase, α2,3-sialidase, α2,3-trans-sialidase acitivities and CMP-Neu5Ac hydrolase activity. It was estimated that it has also α2,6-sialidase activity but this activity in comparison with other four activities is negligible. |
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| Keywords: | N-glycans, glycosyltransferase, Pasteurela dagmagtis, sialyltransferase, N-glycans, sialic acid |
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| Place of publishing: | Maribor |
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| Publisher: | [D. Kokot] |
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| Year of publishing: | 2012 |
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| PID: | 20.500.12556/DKUM-22384 |
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| UDC: | 577.21(043.2) |
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| COBISS.SI-ID: | 16059670 |
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| NUK URN: | URN:SI:UM:DK:DOZYWCAN |
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| Publication date in DKUM: | 22.03.2012 |
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| Views: | 2674 |
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| Downloads: | 82 |
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| Metadata: |    |
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| Categories: | KTFMB - FKKT
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KOKOT, Deja, 2012, PURIFICATION AND BIOCHEMICAL CHARACTERIZATION OF BACTERIAL GLYCOSYLTRANSFERASE [online]. Bachelor’s thesis. Maribor : D. Kokot. [Accessed 28 April 2025]. Retrieved from: https://dk.um.si/IzpisGradiva.php?lang=eng&id=22384
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