Literature summary for 4.6.1.18 extracted from

Arnold, U.; Schulenburg, C.; Schmidt, D.; Ulbrich-Hofmann, R.
Contribution of structural peculiarities of onconase to its high stability and folding kinetics (2006), Biochemistry, 45, 3580-3587.

Search for more literature for 4.6.1.18

Protein Variants

Protein Variants	Comment	Organism
C87A/C104A	66% of wild-type activity, decrease in melting temperature	Lithobates pipiens
F28A	61% of wild-type activity, decrease in melting temperature	Lithobates pipiens
F28T	60% of wild-type activity, decrease in melting temperature	Lithobates pipiens
F36Y	80% of wild-type activity, decrease in melting temperature	Lithobates pipiens
Glp1E	41% of wild-type activity, decrease in melting temperature	Lithobates pipiens
glp1P	44% of wild-type activity, decrease in melting temperature	Lithobates pipiens

Organism

Organism	UniProt	Comment	Textmining
Lithobates pipiens	P22069	-	-

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	the extremely high thermodynamic stability of enzyme is due to a dramatic deceleration of the unfolding reaction	Lithobates pipiens
69.4	-	mutant C87A/C104A, melting temperature	Lithobates pipiens
77.4	-	mutant F28T, melting temperature	Lithobates pipiens
78.1	-	mutant F28A, melting temperature	Lithobates pipiens
79.2	-	mutant F36Y, melting temperature	Lithobates pipiens
87	-	mutant Glp1E, melting temperature	Lithobates pipiens
87.7	-	mutant Glp1P, melting temperature	Lithobates pipiens
88.5	-	wild-type, melting temperature	Lithobates pipiens

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Release 2023.1 (January 2023)