Literature summary for 4.6.1.18 extracted from

Mombelli, E.; Afshar, M.; Fusi, P.; Mariani, M.; Tortora, P.; Connelly, J.P.; Lange, R.
The role of phenylalanine 31 in maintaining the conformational stability of ribonuclease P2 from Sulfolobus solfataricus under extreme conditions of temperature and pressure. (1997), Biochemistry, 36, 8733-8742.

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Protein Variants

Protein Variants	Comment	Organism
F31A	considerable decrease in stability against heat and pressure. Analysis of thermodynamic parameters	Saccharolobus solfataricus
F31Y	considerable decrease in stability against heat and pressure. Analysis of thermodynamic parameters	Saccharolobus solfataricus

General Stability

General Stability	Organism
wild-type enzyme is extremely stable under all conditions of temperature and pressure applied. Thermodynamic analysis of heat and cold denaturation	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	P61991	isoform P2	-

Subunits

Subunits	Comment	Organism
More	strong van der Waals interaction energy between residues F5, F31, and Y33	Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
-20	90	wild-type enzyme is extremely stable under all conditions of temperature and pressure applied. Thermodynamic analysis of heat and cold denaturation	Saccharolobus solfataricus

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Release 2023.1 (January 2023)