EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.107 | C57A/C69A |
mutant represents a completely reduced HtrA being unable to form the intramolecular S-S bond. Mutant very efficiently degrades alkaline phosphatase at 20°C which is very pronounced compared to wild-type. Thus, the reduction of HtrAs disulfide bridge may facilitate the activation of the protease |
700046 |
| 3.4.21.107 | C57S/C69S |
mutant enzyme is less stable, in contrast to wild-type enzyme the mutant protein is autocleaved even without reducing agents |
650414 |
| 3.4.21.107 | D221A |
mutant displays reduced peptide Tyr-Tyr-Phe-stimulated cleavage activity |
732925 |
| 3.4.21.107 | D221A/H198P |
mutant displays more than 65% of peptide Tyr-Tyr-Phe-stimulated cleavage activity of mutant H198P |
732925 |
| 3.4.21.107 | D232V |
the mutation causes a stimulation of proteolytic activity |
711014 |
| 3.4.21.107 | D52A |
mutation within LA loop. Mutation has no impact on the proteolytic activity of HtrA |
732134 |
| 3.4.21.107 | D53A |
mutation within LA loop. Mutation has no impact on the proteolytic activity of HtrA |
732134 |
| 3.4.21.107 | DELTA360-448 |
mutant lacking the PDZ2 domain. Results of gel filtration reveal that the removal of the whole PDZ2 domain, results in the formation of only trimers that form neither the hexamers nor the 12- or 24-mers. Such a mutant trimeric form of DegP exhibits both chaperone-like and protease activities at a level comparable to that of the wild-type protein. Mutant shows no concentration effect compared to wild-type |
700942 |
| 3.4.21.107 | DELTA440-448 |
the removal of the beta26 strand on the C terminus of the PDZ2 domain (residues 440-448), which is shown to directly interact with the neighboring PDZ1 domain, does not disrupt the formation of DegP hexamers but prevents their conversion to the 12- or 24-mers. Mutant protein exhibits significantly lower chaperone-like and protease activity, suggesting an inhibitory role of the PDZ2 domain for DegP to exhibit chaperone and protease activities. Mutant shows no concentration effect compared to wild-type |
700942 |
| 3.4.21.107 | E384K |
naturally occuring single missense mutation in Rhodobacter capsulatus DsbA-null mutant revertant, the mutation leads to decreased protease activity, structural model |
683875 |
