Expression of glycosyltransferase in fussion with MBP and following TEV protease cleavage

Kód výsledku v 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>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Expression of glycosyltransferase in fussion with MBP and following TEV protease cleavage

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Expression of glycosyltransferase in fussion with MBP and following TEV protease cleavage

Popis výsledku anglicky

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.

Druh

O - Ostatní výsledky

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů