EC Number   |
Activating Compound |
Reference |
|---|
   3.1.26.5 | 2-methyl-2,4-pentanediol |
enhances cleavage reaction of the M1 RNA subunit alone |
134422 |
| 3.1.26.5 | erythromycin |
- |
678342 |
| 3.1.26.5 | more |
enzyme requires low salt levels |
654201 |
| 3.1.26.5 | more |
enzyme requires very high salt levels |
654201 |
| 3.1.26.5 | more |
ribosomal protein L7Ae is a subunit of archaeal RNase P. Addition of L7Ae to this RNase P complex increases the optimal reaction temperature and kcat/Km (by approximately 360fold) for pre-tRNA cleavage to those observed with partially purified native enzyme |
728660 |
| 3.1.26.5 | more |
the pre-tRNA leaderprotein interaction decreases the observed dissociation rate of pre-tRNA from the isomerized enzyme-substrate complex |
710549 |
| 3.1.26.5 | more |
the RNR motif enhances catalytic activity and substrate recognition, it enhances the affinity of RNase P for pre-tRNA involving residues R60 and R62, overview |
716901 |
| 3.1.26.5 | PhoPop5 protein |
PhoPop5 is an archaeal homolog of human RNase P protein hPop5 involved in the activation of RNase P RNA in the hyperthermophilic archaeon Pyrococcus horikoshii. Extra-structural elements in the RNA recognition motif in PhoPop5 play a crucial role in the activation, that is, the C-terminal extension in the dimerized PhoPop5 protein through the loop between alpha1 and alpha2 is essential for the activation of the enzyme by promoting RNA annealing and RNA strand displacement |
724195 |
| 3.1.26.5 | Polyethylene glycol |
enhances cleavage reaction of the M1 RNA subunit alone |
134422 |
| 3.1.26.5 | protein PhoPop5 |
the enzyme is enzymatically active only when bound to proteins PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30 |
744218 |
