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Mechanistic and Evolutionary Analyses of the Sialic Acid Synthase Family

Sialic acids are prevalent in many organisms and facilitate a range of cellular processes in both bacteria and mammals. Whilst a variety of sialic acids are present in nature, N-Acetylneuraminic acid (NANA) is the most common and plays a key role in the pathogenesis of a select number of neuroinvasive bacteria such as Neisseria meningitidis. These pathogens coat themselves with polysialic acids, mimicking the exterior surface of mammalian cells and consequentially concealing the bacteria from the host’s immune system. NANA is synthesised in prokaryotes via a condensation reaction between phosphoenolpyruvate and N-acetylmannosamine. This reaction is catalysed by the domain swapped, homodimeric enzyme, N-acetylneuraminic acid synthase (NANAS). Each NANAS monomer is comprised of two distinct domains; a catalytic domain linked to an antifreeze protein-like (AFPL) domain. This thesis outlines research into the role of the AFPL domain using a range of structural and kinetic analyses to compare variant enzymes to the natural, NmeNANAS enzyme. An investigation was also made into the evolutionary relationships between NANAS and other bacterial sialic acid synthases such as Legionaminic acid synthase and Pseudaminic acid synthase.

Identiferoai:union.ndltd.org:canterbury.ac.nz/oai:ir.canterbury.ac.nz:10092/9059
Date January 2014
CreatorsJoseph, Dmitri Daniel Alexander
PublisherUniversity of Canterbury. Chemistry
Source SetsUniversity of Canterbury
LanguageEnglish
Detected LanguageEnglish
TypeElectronic thesis or dissertation, Text
RightsCopyright Dmitri Daniel Alexander Joseph, http://library.canterbury.ac.nz/thesis/etheses_copyright.shtml
RelationNZCU

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