EC Number |
Protein Variants |
Reference |
---|
3.1.3.52 | A193X |
single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutant demonstrate basal activity against branched-chain alpha-keto dehydrogenase (BCKD) but impaired responsiveness to branched-chain-alpha-keto acids (BCKAs) |
732061 |
3.1.3.52 | E321K |
single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutant demonstrate basal activity against branched-chain alpha-keto dehydrogenase (BCKD) but impaired responsiveness to branched-chain-alpha-keto acids (BCKAs). Mutant is not detected by immunoblot using human PP2Cm antibody. Therefore, it remains unclear whether this mutant is phosphatase dead due to loss-of-function mutations or unstable due to premature truncation |
732061 |
3.1.3.52 | F359X |
single-nucleotide polymorphisms (SNPs) in human PP2Cm: frameshift mutant shows no phosphatase activity at basal or after branched-chain-alpha-keto acids (BCKA) treatment. Mutant is not detected by immunoblot using human PP2Cm antibody. Therefore, it remains unclear whether this mutant is phosphatase dead due to loss-of-function mutations or unstable due to premature truncation |
732061 |
3.1.3.52 | I167T |
single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutation has no an elevated activity compared to wild-type |
732061 |
3.1.3.52 | more |
motifs responsible for PP2Cm and E2 interaction: using deletion mutants it is shown that the region between the residues 46 and 61 is critical to the association of PP2Cm with the complex |
732061 |
3.1.3.52 | N94K |
missense mutant due to single nucleotide polymorphism. Mutation significantly impairs Mg2+-dependent catalytic activity and induces a conformational change in the key residue in coordinating the Mg2+ in the active site |
751367 |
3.1.3.52 | N94K |
single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutation has no impact on PP2Cm activity |
732061 |