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Permanent link (DOI): https://doi.org/10.7939/R3N58CX43

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Preparation and enzymatic recognition of α-D-mannopyranosyl-1-phosphate analogs Open Access

Descriptions

Other title
Subject/Keyword
Mycobacterium tubeculosis
polyprenol phosphate analogs
mannopyranosyl-1-phosphate analogs
kinetic analysis
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Zou, Lu
Supervisor and department
Lowary, Todd L. (Chemistry)
Examining committee member and department
Cairo, Christopher W. (Chemistry)
Velazquez, Carlos A. (Pharmacy and Pharmaceutical Sciences)
Department
Department of Chemistry
Specialization

Date accepted
2012-06-08T15:04:48Z
Graduation date
2012-06
Degree
Master of Science
Degree level
Master's
Abstract
Tuberculosis is a contagious disease, caused by Mycobacterium tuberculosis. Harsh requirements required to treat tuberculosis result from the structure of the mycobacterial cell wall. Lipoarabinomannan, an important component and major antigen of the cell wall, is able to modulate the host immune response. Among the glycosyltransferases that involved in LAM biosynthesis, a PPM-dependent α-(1→6)-ManT that transfers a mannose residue from a PPM donor to an oligosaccharide acceptor has been a research focus in our group. The PPM donor used by this enzyme is biosynthesized from mannose-1-phosphate by the action of a GDP-ManPP and a PPM synthase. To better understand how these enzymes interact with the mannose substrates, a series of methoxy and deoxy derivatives of mannose-1-phosphate were synthesized, then converted into the corresponding GDP-Man analogs. Steric interactions and hydrogen-bonding was mapped using an established colorimetric assay. Additionally, a PPM analog was synthesized and shown to be substrate for PPM synthase.
Language
English
DOI
doi:10.7939/R3N58CX43
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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