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Literature summary for 2.6.1.44 extracted from

  • Oppici, E.; Roncador, A.; Montioli, R.; Bianconi, S.; Cellini, B.
    Gly161 mutations associated with Primary Hyperoxaluria Type I induce the cytosolic aggregation and the intracellular degradation of the apo-form of alanine:glyoxylate aminotransferase (2013), Biochim. Biophys. Acta, 1832, 2277-2288.
    View publication on PubMed
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Application

Application Comment Organism
medicine mutations in conserved residue Gly161 to Arg, Cys or Ser are associated with Primary Hyperoxaluria Type I, a severe rare disorder of metabolism. Mutations of Gly161 strongly reduce the expression levels and the intracellular half-life of AGT, and make the protein in the apo-form prone to an electrostatically-driven aggregation in the cell cytosol. The coenzyme pyridoxal 5'-phospahte, by shifting the equilibrium from the apo- to the holo-form, is able to reduce the aggregation propensity of the variants, thus partly decreasing the effect of the mutations Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression in CHO cell Homo sapiens

Protein Variants

Protein Variants Comment Organism
G161C 5% of wild-type expression level, reduced catalytic activity Homo sapiens
G161R 4% of wild-type expression level, reduced catalytic activity Homo sapiens
G161S 12% of wild-type expression level, reduced catalytic activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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