Characterization of aspartate N-acetyltransferase and search of the catalytic activity of other proteins from the same family

Tahay, Gaƫlle
(2015)

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Authors
  • Tahay, GaĆ«lleUCLouvain
    author
Supervisors
Van Schaftingen, Emile
Abstract
N-acetylaspartate (NAA) is the second most abundant organic compound in brain, though its function remains mysterious. The first aim of my thesis was to better characterize the enzyme (NAT8L) that synthesizes it. Site-directed mutagenesis allowed us to identify some of the residues that are important for the enzymatic activity. We also showed that NAT8L is associated with the endoplasmic reticulum (ER) thanks to a hydrophobic region that presumably forms a loop in the ER membrane. The second aim of my work was to discover the function of three other mammalian proteins belonging to the GNAT family. Like NAT8L, NAT14 was found to be associated with the ER, but its catalytic activity could not be identified. The methionine-sulfone N-acetyltransferase activity of NAT9 preparations could be ascribed to a bacterial contaminant identified as YncA.
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Citations

Tahay, G. (2015). Characterization of aspartate N-acetyltransferase and search of the catalytic activity of other proteins from the same family. https://hdl.handle.net/2078.5/186889