EC Number   |
Protein Variants |
Reference |
|---|
    5.3.99.2 | A106S |
creation of a new protein kinase C phosphorylation site, significant inhibition of the ability of enzyme to induce apoptosis and significant decrease in catalytic activity |
682619 |
| 5.3.99.2 | C156L |
loss of prostaglandin D synthase activity, retention of glutathione S-transferase activity |
652044 |
| 5.3.99.2 | C156Y |
loss of prostaglandin D synthase activity, retention of glutathione S-transferase activity |
652044 |
| 5.3.99.2 | C186A |
mutant is properly folded with well-defined tertiary structures |
690222 |
| 5.3.99.2 | C186A |
no significant change in conformation. Decrease in stability and in dissociation constants for 8-anilino-1-naphthalenesulfonic acid and retinoic acid. Urea-induced unfolding at 2.875 mol/l compared with 5.75 mol/l for wild-type |
691128 |
| 5.3.99.2 | C65A |
inactive |
714938 |
| 5.3.99.2 | C65A |
mutant binds all-trans-retinoic acid, bilirubin and biliverdin with high affinity. Radius of gyration is 19.4 A for the free enzyme, and it become compact after binding of these ligands |
692921 |
| 5.3.99.2 | C65A |
mutant is properly folded with well-defined tertiary structures |
690222 |
| 5.3.99.2 | C65A |
mutation of active site, significant inhibition of the ability of enzyme to induce apoptosis and significant decrease in catalytic activity |
682619 |
| 5.3.99.2 | C65A |
no significant change in conformation. Urea-induced unfolding at 5.125 mol/l compared with 5.75 mol/l for wild-type |
691128 |
