Expression of glycosyltransferase in fussion with MBP and following TEV protease cleavage
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F11%3A00053914" target="_blank" >RIV/00216224:14740/11:00053914 - 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
Expression of glycosyltransferase in fussion with MBP and following TEV protease cleavage
Original language description
Members of the genus Mycobacterium are responsible for major health problems in humans. Mycobacterium tuberculosis is gram positive, acid resistent bacterium causing chronic illness. Due to the essentiality of mycobacterial cell wall, the enzymes responsible for its synthesis pose a wellcome target for design of new therapeutics. Rv3782 is galactofuranosyl transferase responsible for attaching the first and, perhaps, the second Galf unit to the C50-P-P-GlcNAc-Rha acceptor in the biosynthetic pathway ofarabinogalactan. Glycosyltransferases are in general notoriously difficult to express and purify. Several expression-purification strategies have been applied on this enzyme without satisfying outcome. Modified scheme for purification of Rv3782 for structure-functional studies will be presented. Expression of MBP, TEV cleavage site and Rv3782 in one polypeptide chain faciliated by recombinant DNA techniques could lead to successfull purification of Rv3782.
Czech name
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Czech description
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Classification
Type
O - Miscellaneous
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů