EC Number   |
Protein Variants |
Reference |
|---|
    1.11.1.11 | A143P |
site-directed mutagenesis of the delta-site of substrate oxidation, the electronic absorption spectra and dissociation constants for binding of cyanide and azide to the isolated heme are not significantly different for the mutant compared to wild-type, also the rate constants in the peroxidase reaction mechanism are not significantly affected by the replacement of A134 by proline. The insertion of a proline does not substantially alter the product distribution in APX |
765196 |
| 1.11.1.11 | C126A |
kcat/KM for L-ascorbate is 1.4fold higher than wild-type enzyme. kcat/Km for H2O2 is 1.7fold lower than wild-type enzyme |
684930 |
| 1.11.1.11 | C25S |
kcat/Km for L-ascorbate is 5.4fold lower than wild-type value. kcat/KM for H2O2 is 2.1fold lower than wild-type value. In contrast to wild-type enzyme, the mutant enzyme retains more than 90% of the initial activity after incubation for 10 min with the radical scavenger 2,2,6,6-tetramethylpiperidinyl-1-oxy and H2O2 |
686710 |
| 1.11.1.11 | C25S/C121S |
kcat/Km for L-ascorbate is 4.5fold lower than wild-type value. kcat/KM for H2O2 is 2.1fold lower than wild-type value. In contrast to wild-type enzyme, the mutant enzyme retains more than 90% of the initial activity after incubation for 10 min with the radical scavenger 2,2,6,6-tetramethylpiperidinyl-1-oxy and H2O2 |
686710 |
| 1.11.1.11 | C26S |
kcat/KM for L-ascorbate is 1.8fold lower than wild-type enzyme. kcat/Km for H2O2 is 3.1fold lower than wild-type enzyme |
684930 |
| 1.11.1.11 | C26S |
kcat/Km for L-ascorbate is 1.8fold lower than wild-type value. kcat/KM for H2O2 is 3.1fold lower than wild-type value. In contrast to wild-type enzyme, the mutant enzyme retains 60% of the initial activity after incubation for 10 min with the radical scavenger 2,2,6,6-tetramethylpiperidinyl-1-oxy and H2O2 |
686710 |
| 1.11.1.11 | C26S/C126A |
kcat/KM for L-ascorbate is 1.3fold lower than wild-type enzyme. kcat/Km for H2O2 is 2.5fold lower than wild-type enzyme |
684930 |
| 1.11.1.11 | C26S/W35F/C126A |
kcat/KM for L-ascorbate is 1.6fold than wild-type enzyme. kcat/Km for H2O2 is 3.4fold lower than wild-type enzyme. Mutant shows increased tolerance to H2O2 (retains 50% of the initial activity after H2O2 treatment for 3 min) compared to wild-type enzyme (half-time of inactivation is less than 10 sec) |
684930 |
| 1.11.1.11 | C32S |
the mutation leads to approximately 70% drop in ascorbate peroxidase activity with no effect on guaiacol peroxidase activity, these results indicate that uncharged aromatic substrates and the anionic ascorbate molecule interact with different sites on the enzyme |
439873 |
| 1.11.1.11 | CCP2APX |
residues 30-42, LREDDEYDNYIGY, of wild-type CCP are replaced with residues 27-32, IAEKKC, of APX in order to introduce the ascorbate-binding loop, a N184R point mutation is added |
696216 |
