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Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F02%3A00007110" target="_blank" >RIV/00216224:14310/02:00007110 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome

  • Original language description

    Mycobacterium tuberculosis is a pathogen that is resistant to most common antibiotics and chemotherapeutic agents. This resistance is related to an unusual and well-organized structure of the mycobacterial cell wall that shows an abnormally low degree ofthe hydrophilic permeability. Outer cell wall contains the biochemically unique structures of sugar residues, constituents of various branched and complex polysaccharides and glycolipids . There is very little knowledge about the biosynthesis pathways of these glycoconjugates and about the enzymes, especially glycosyltransferases (GT), involved. The genome of M. tuberculosis contains 3,951 protein-coding sequences. Putative function annotation of some of them was predicted using a combination of sequence alignment and motif comparison . Using this approach, only a small number of putative GTs was identified. Recent crystal structure determination of GTs demonstrated that they adopt only a limited number of topology . We focused on 3D-t

  • Czech name

  • Czech description

Classification

  • Type

    D - Article in proceedings

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/LN00A016" target="_blank" >LN00A016: BIOMOLECULAR CENTER</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2002

  • Confidentiality

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

Data specific for result type

  • Article name in the collection

    XIXčmes Journées de Chimie et Biochimie des Glucides

  • ISBN

  • ISSN

  • e-ISSN

  • Number of pages

    1

  • Pages from-to

    65

  • Publisher name

    Societe francaise de Chimie

  • Place of publication

    France

  • Event location

    May 20 - 24, Albe, France

  • Event date

  • Type of event by nationality

    EUR - Evropská akce

  • UT code for WoS article