The taxonomic range for the selected organisms is: Saccharomyces cerevisiae The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
wild type enzyme activity drastically decreases by addition of 0.2 mM L-Arg, and consequently decreases when L-Arg concentration is increased, indicating that the enzyme activity is subject to feedback inhibition by L-Arg. Enzyme activity is almost lost in the presence of 1.0 mM L-Arg
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of both the DUF619 domain-lacking yNAGK, ligand-free as well as complexed with acetylglutamate or acetylglutamate and arginine, and of complete mature yNAGK are determined. yNAGK has as central structure a flat tetramer formed by two dimers of amino acid kinase domains
truncated mutant lacking C-terminal 150 amino acids (spanning residues 38-356), belonging to the DUF619 domain family, shows that is it stabilizes yNAGK, slows catalysis and modulates feed-back inhibition by arginine. Truncated yNAGK shows doubled kcat compared to wild-type, Km is almost not affected. IC50 (L-arginine) is lowered compared to wild-type. Truncated mutand shows lower thermal stability compared to wild-type
Abadjieva, A.; Pauwels, K.; Hilven, P.; Crabeel, M.
A new yeast metabolon involving at least the two first enzymes of arginine biosynthesis. Acetylglutamate synthase activity requires complex formation with acetylglutamate kinase
Pauwels, K.; Abadjieva, A.; Hilven, P.; Stankiewicz, A.; Crabeel, M.
The N-acetylglutamate synthase/N-acetylglutamate kinase metabolon of Saccharomyces cerevisiae allows co-ordinated feedback regulation of the first two steps in arginine biosynthesis
High-level production of ornithine by expression of the feedback inhibition-insensitive N-acetyl glutamate kinase in the sake yeast Saccharomyces cerevisiae