EC Number   |
Protein Variants |
Reference |
|---|
    3.1.3.2 | A385V |
mutation in metallophosphatase domain results in complete loss of enzymatic activity |
716625 |
| 3.1.3.2 | D100A |
1% wild-type activity |
701794 |
| 3.1.3.2 | D167N |
mutation in metallophosphatase domain results in complete loss of enzymatic activity |
716625 |
| 3.1.3.2 | D66N |
D66N, a mutant of P4 in which the residue that protonates the leaving group (Asp66) is changed to Asn, is used for structure determination of enzyme-substrate complexes. Structures of D66N complexed with nicotinamide mononucleotide and 5'-AMP are determined at high-resolution limits of 1.35 A and 1.55 A, respectively |
715922 |
| 3.1.3.2 | D73N |
the mutation effaces RNase H activity but has virtually no effect on the acid phosphatase activity of the RnhC protein |
750957 |
| 3.1.3.2 | DELTAN47 |
ratio of turnover number to Km-value is 20.7fold lower than that of wild-type enzyme |
649472 |
| 3.1.3.2 | DELTAN62 |
ratio of turnover number to Km-value is more than 5650000fold lower than that of wild-type enzyme |
649472 |
| 3.1.3.2 | DELTAN88 |
ratio of turnover number to Km-value is more than 5650000fold lower than that of wild-type enzyme |
649472 |
| 3.1.3.2 | E340K |
mutation in metallophosphatase domain results in complete loss of enzymatic activity |
716625 |
| 3.1.3.2 | E363K |
mutation in metallophosphatase domain results in complete loss of enzymatic activity |
716625 |
