EC Number   |
Protein Variants |
Reference |
|---|
    2.4.2.28 | A15M |
the mutant shows 14.5% catalytic efficiency compared to the wild type enzyme |
726889 |
| 2.4.2.28 | C136S |
mutant is insensitive to oxidative inhibition |
684999 |
| 2.4.2.28 | C223S |
mutant is insensitive to oxidative inhibition |
684999 |
| 2.4.2.28 | C259S/C261S |
in contrast wo wild-type C262S and C259S/C261S mutants show complete thermal denaturation curves with sigmoidal transitions centered at 102°C and 99°C respectively. Under reducing conditions these values decrease by 4°C and 8°C respectively, highlighting the important role exerted by the CXC disulfide on enzyme thermostability. The double mutant (the mutant lacking the structural CXC motif), has more impact on the thermostability of SsMTAPII than the single mutant |
721732 |
| 2.4.2.28 | C259S/C261S |
mutant enzyme shows thermophilic and thermostable features significantly lower than those of the wild-type enzyme |
658681 |
| 2.4.2.28 | C259S/C261S |
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 102°C. Specific activity is similar to the activity of the wild-type enzyme |
-, 731366 |
| 2.4.2.28 | C259S/C261S/C262S |
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 91°C. Specific activity is similar to the activity of the wild-type enzyme |
-, 731366 |
| 2.4.2.28 | C259S/C261S/C262S/C200S/C205S |
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 73°C. Specific activity is similar to the activity of the wild-type enzyme |
-, 731366 |
| 2.4.2.28 | C259S/C261S/C262S/C200S/C205S/C138S |
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 78°C. Specific activity is similar to the activity of the wild-type enzyme |
-, 731366 |
| 2.4.2.28 | C259S/C261S/C262S/C200S/C205S/C138S/C164S |
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 73°C. Specific activity is similar to the activity of the wild-type enzyme |
731366 |
