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EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Reference
3.1.26.5
-999
-
circular dichroism thermal denaturation studies of P protein (noncatalytic component of ribonuclease P) in the presence of stabilizing solute (osmolyte or ligand) to obtain a thermodynamic description of temperature-induced unfolding of the ligand-folded and trimethylamine N-oxide-folded conformations of P protein
664073
3.1.26.5
-999
-
mutations which affect either the protein or RNA component of RNase P can confer thermal sensitivity on the enzyme both in vivo and in vitro. The protein component of RNase P from ts241 and the RNA component of RNase P from ts709, respectively, account for the thermal sensitivity of the RNase P from the two strains
134429
3.1.26.5
-999
-
ribosomal protein L7Ae increases the thermostability of the RNase P holoenzyme, the secondary structure is not different from that of the wild type enzyme
728660
3.1.26.5
67
-
Tm-value of the protein component
134454
3.1.26.5
999
-
thermostable
678540
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