EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.92 | E8R/R12E/E14R/R15E |
residues 8-15 form the channel loop of the pore: when charged residues in the channel (amino acids 8-15) are reversed this mutant cleaves the decapeptide at a rate 8fold faster than observed with wild-type ClpP but cleaves the dipeptide at a comparable rate. Mutant shows a much slower degradation of GFP-ssrA |
717989 |
| 3.4.21.92 | G127 |
mutant shows no activity |
717089 |
| 3.4.21.92 | G128 |
mutant shows no activity |
717089 |
| 3.4.21.92 | G131 |
mutant shows no activity |
717089 |
| 3.4.21.92 | G773R |
inactive mutant |
717092 |
| 3.4.21.92 | H230A |
RKH mutant to investigate the role of the RKH sequence loops |
683865 |
| 3.4.21.92 | I19A |
mutant shows wild-type level of dipeptide cleavage, 20fold increase in decapeptide cleavage compared to wild-type, in contrast to wild-type mutant degrades 113-residue unfolded I27 domain of human titin. Mutant shows high decrease in ClpX affinity |
717989 |
| 3.4.21.92 | I19D |
mutant shows 16fold increase in decapeptide cleavage compared to wild-type |
717989 |
| 3.4.21.92 | I19L |
mutant shows 6fold increase in decapeptide cleavage compared to wild-type |
717989 |
| 3.4.21.92 | K229A |
RAH mutant to investigate the role of the RKH sequence loops |
683865 |
