EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.92 | R22A |
mutant shows wild-type level of dipeptide cleavage, 1.5fold increase in decapeptide cleavage compared to wild-type. Mutant shows high decrease in ClpX affinity |
717989 |
| 3.4.21.92 | S101A |
mutation of the active site Ser-101 in ClpP3 inactivates the entire ClpCP3/R protease, the mutation has no effect on the formation of the recombinant ClpP3/R core complex of 270 kDa. The mutated ClpP3/R complex stimulates the steady-state ATPase activity of ClpC to the same extent as wild-type ClpP3/R. The mutated ClpP3/R core fails to degrade the alpha-casein nor the more sensitive FITC-casein |
698890 |
| 3.4.21.92 | S21A |
mutant shows wild-type level of dipeptide cleavage, 5fold increase in decapeptide cleavage compared to wild-type. Mutant shows high decrease in ClpX affinity |
717989 |
| 3.4.21.92 | S499C |
mutation introduced for FRET measurements. Labelling of S499C with fluorescent probes induces a 10-20fold increase in both chaperone and ATPase activities |
-, 752706 |
| 3.4.21.92 | S61A/Y63V/L83A/Y91V |
mutations in hydrophobic patch of subunit ClpP1. Complex formation and processing still occurs. The complex containing the mutant is catalytically active |
755086 |
| 3.4.21.92 | S97A |
inactive. Overexpression has no effect on sensitivity of cells to cisplatin |
752813 |
| 3.4.21.92 | S98A |
inactive trapping variant |
-, 754888 |
| 3.4.21.92 | S98A |
mutant shows no activity |
717089 |
| 3.4.21.92 | S99A |
does not digest peptide into smaller fragments |
699539 |
| 3.4.21.92 | Y20A |
mutant shows wild-type level of dipeptide cleavage, 5fold increase in decapeptide cleavage compared to wild-type. Mutant shows high decrease in ClpX affinity |
717989 |
