EC Number   |
Protein Variants |
Reference |
|---|
   3.4.17.12 | E260A |
mutation reduces the ratio of turnover-numver to Km-value by 104fold and further decreases stability.Addition of 0.5 M NaCl to the assay buffer does not significantly alter the activities of the wild-type enzyme with 0.2 mM dansyl-Ala-Arg or the E260Q mutant enzyme but does substantially increase the activity of the E260A mutant, 219%. The enhancement of E260A is not specific for NaCl, as similar increases are detected with other salts such as NaNO3, 249%, KNO3, 256%, KCl, 256%, or Na2SO4, 297% |
647255 |
| 3.4.17.12 | E260Q |
mutation has minimal effects on kinetic parameters, but decreased heat stability |
647255 |
| 3.4.17.12 | E264Q |
mutation results in a 10000fold decrease in activity, but the enzyme still binds to p-aminobenzoylarginine-Sepharose and is resistant to trypsin treatment, indicating that the protein is folded properly |
647255 |
| 3.4.17.12 | E264Q |
the mutation completely eliminates the CPM activity |
697395 |
| 3.4.17.12 | S406A |
very similar to the wild-type enzyme with regard to expression and release by phosphatidylinositol-specific phospholipase C |
647255 |
| 3.4.17.12 | S406P |
the wild-type and S406A and S406T mutants are expressed on the plasma membrane in glycosylphosphatidylinositol-anchored form, the S406P mutant is not and is retained in a perinuclear location |
647255 |
| 3.4.17.12 | S406T |
very similar to the wild-type enzyme with regard to expression and release by phosphatidylinositol-specific phospholipase C |
647255 |
