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Glutamine synthetase in Bacteroides fragilis

Includes bibliographical references (p. 78-90).

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Bibliographic Details
Main Author: Tumba, Nancy
Other Authors: Abratt, Valerie Rose
Format: Thesis
Language:English
Published: Department of Molecular and Cell Biology 2015
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access_status_str Open Access
author Tumba, Nancy
author2 Abratt, Valerie Rose
author_browse Abratt, Valerie Rose
Tumba, Nancy
author_facet Abratt, Valerie Rose
Tumba, Nancy
author_sort Tumba, Nancy
collection Thesis
description Includes bibliographical references (p. 78-90).
format Thesis
id oai:open.uct.ac.za:11427/14720
institution University of Cape Town (South Africa)
language eng
last_indexed 2026-06-10T12:39:03.958Z
license_str Not specified — see source repository
provenance_str_mv Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository
publishDate 2015
publishDateRange 2015
publishDateSort 2015
publisher Department of Molecular and Cell Biology
publisherStr Department of Molecular and Cell Biology
record_format dspace
source_str UCTD — University of Cape Town Open Access Repository
spelling oai:open.uct.ac.za:11427/14720 Glutamine synthetase in Bacteroides fragilis Tumba, Nancy Abratt, Valerie Rose Molecular and Cell Biology Includes bibliographical references (p. 78-90). Bactereroides fragilis is a gram-negative, non spore-forming, obligate anaerobe of the human intestinal microbiota. It is, however, an opportunistic pathogen and has been ranked as the most prevalent isolate in cases of anaerobic septicaemia. Similar to most bacteria, ammonium is assimilated in B. fragilis through the action of glutamine synthetase (GS). Glutamine is vital to nitrogen metabolism as it serves as a precursor to many secondary metabolites. GS enzymes are, therefore, vital to the growth of the organism and many prokaryotes are known to possess two or more isoforms of the enzyme. In addition, GS expression and regulation is usually tightly regulated in concert with the availability of nitrogen. Previous studies have identified a single GSIII encoding gene (glnN) in B. fragilis. In this dissertation, an additional ORF coding for a putative GSI enzyme in B. fragilis was identified, isolated and functionally characterized. A putative regulatory protein was also identified and its functional contribution to nitrogen metabolism was determined, in order to extend our understanding of nitrogen assimilation in B. fragilis. 2015-11-08T04:59:11Z 2015-11-08T04:59:11Z 2007 Master Thesis Masters MSc http://hdl.handle.net/11427/14720 eng application/pdf Department of Molecular and Cell Biology Faculty of Science University of Cape Town
spellingShingle Molecular and Cell Biology
Tumba, Nancy
Glutamine synthetase in Bacteroides fragilis
thesis_degree_str Master's
title Glutamine synthetase in Bacteroides fragilis
title_full Glutamine synthetase in Bacteroides fragilis
title_fullStr Glutamine synthetase in Bacteroides fragilis
title_full_unstemmed Glutamine synthetase in Bacteroides fragilis
title_short Glutamine synthetase in Bacteroides fragilis
title_sort glutamine synthetase in bacteroides fragilis
topic Molecular and Cell Biology
url http://hdl.handle.net/11427/14720
work_keys_str_mv AT tumbanancy glutaminesynthetaseinbacteroidesfragilis