EC Number   |
General Stability |
Reference |
|---|
    2.6.1.44 | human AGT can substitute for function of yeast Agx1 (Yeast alanine:glyoxylate aminotransferase) and that mutations associated with disease in humans show reduced growth in yeast. The reduced growth of minor allele mutants reflects reduced protein levels, indicating that these proteins are less stable than wild-type AGT in yeast |
687769 |
| 2.6.1.44 | major allele (P11/I340) is more stable against increasing urea concentrations than minor allele (P11L/I340M) or mutant protein P11L/I340M/G170R |
721754 |
| 2.6.1.44 | partial digestion by trypsin provides an indicator of proper folding of the enzyme, while for some mutants, sensitivity to trypsin can be ameliorated by addition of pyridoxal 5'-phosphate or aminooxyacetic acid |
689026 |
| 2.6.1.44 | partial trypsin digestion provides an indicator of proper folding of the mutant enzyme. For selected mutations the sensitivity to trypsin can be ameliorated by addition of pyridoxal phosphate or aminooxy acetic acid as specific pharmacological chaperones |
689026 |
| 2.6.1.44 | pyridoxal 5'-phosphate stabilizes during purification |
640074 |
