EC Number   |
Protein Variants |
Reference |
|---|
    3.5.4.4 | C27Q/L227I |
the mutation promotes crystallization via crystal packing and to prevents intermolecular disulfide bond formation. The surface engineered enzyme is kinetically comparable to the wild type enzyme |
755901 |
| 3.5.4.4 | C294S |
the wild-type and the C294S mutant strains are stable after heating for 10 min at 60°C |
-, 727779 |
| 3.5.4.4 | D172 |
mutant is 40% less active than the wild-type. Mutant is more thightly bound to erythro-9-(2-hydroxy-3-nonly)adenine (Ki: 0.0009 mM) than wild-type |
718893 |
| 3.5.4.4 | D172A |
the mutant shows no activity with 5-methylthioadenosine and is not inhibited by 5'-methylthiocoformycin |
711215 |
| 3.5.4.4 | D172E |
the mutant shows no activity with 5-methylthioadenosine and is not inhibited by 5'-methylthiocoformycin |
711215 |
| 3.5.4.4 | D176A |
mutation reduces adenosine and 5'-methylthioadenosine substrate affnity |
755901 |
| 3.5.4.4 | D176M |
mutation reduces adenosine and 5'-methylthioadenosine substrate affnity |
755901 |
| 3.5.4.4 | E150R |
less thermostable than wild-type enzyme, stable for only 10 min at 50°C |
-, 727779 |
| 3.5.4.4 | F136L |
mutant enzyme shows increased Km (more than 10fold) for adenosine and 5'-methylthioinosine |
755901 |
| 3.5.4.4 | M155D |
mutation reduces kcat |
755901 |
