EC Number   |
Application |
Reference |
|---|
    2.6.1.44 | analysis |
development of an indirect glycolate cytotoxicity assay using CHO cells expressing glycolate oxidase and various normal and mutant forms of AGT |
737777 |
| 2.6.1.44 | diagnostics |
loss of AGXT expression is correlated with a poor prognosis and differentiation of hepatocellular carcinoma (HCC) |
759686 |
| 2.6.1.44 | medicine |
- |
640075, 640078, 640081, 640086, 640087, 640088 |
| 2.6.1.44 | medicine |
after 4 weeks of vitamin B6-deficient diet, hepatic enzyme activity and mRNA level are significantly lower than in control animals. Urinary oxalate-to-creatinine and glycolate-to-creatinine ratios are higher than in controls, but urinary glycine-to-creatinine and citrate-to-creatinine ratios are significantly lower |
662732 |
| 2.6.1.44 | medicine |
hereditary disease primary hyperoxaluria type 1 is caused by a deficiency of the liver-specific peroxisomal enzyme alanine:glyoxylate aminotransferase, diagnosis with selective inhibitors and enzyme assays |
640076, 640079, 640084 |
| 2.6.1.44 | medicine |
infusion of asymmetric dimethylarginines causes a 3- to 4fold increase in plasma and urine asymmetric dimethylarginine levels and a 2- to 3fold increase in plasma and urine levels of the asymmetric dimethylarginine-specific metabolite of AGXT2, alpha-keto-delTA-(N,N-dimethylguanidino)valeric acid. Plasma levels of alpha-keto-delTA-(N,N-dimethylguanidino)valeric acid are elevated 32fold in the mice, which underwent bilateral nephrectomy. Neither bilateral nephrectomy nor asymmetric dimethylarginine infusion causes upregulation of AGXT2 expression or activity |
739170 |
| 2.6.1.44 | 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 |
737740 |
| 2.6.1.44 | medicine |
primary hyperoxaluria type I is a severe kidney stone disease caused by mutations in the protein alanine:glyoxylate aminotransferase |
687769 |
| 2.6.1.44 | medicine |
the effectiveness of pharmacological doses of pyridoxine results froman improved metabolic effectiveness of AGT. In cells expressing glycolate oxidase the great majority of glycolate is converted to oxalate and glyoxylate, with the latter causing the greater decrease in cell survival. Co-expression of normal AGTs and some, but not all, mutant AGT variants partially counteracts this cytotoxicity and leads to decreased synthesis of oxalate and glyoxylate. Increasing the extracellular pyridoxine up to 0.3 microM leads to an increased metabolic effectiveness of normal AGTs and the G170R variant. The increased survival seen with G170R is paralleled by a 40% decrease in oxalate and glyoxylate levels |
737777 |
| 2.6.1.44 | nutrition |
overexpression of enzyme in Ashbya gossypii, use for production of riboflavin for human and animal feed supplement |
660780 |
