Literature summary for 4.6.1.18 extracted from

K�ditz, J.; Ulbrich-Hofmann, R.; Arnold, U.
Probing the unfolding region of ribonuclease A by site-directed mutagenesis (2004), Eur. J. Biochem., 271, 4147-4156.

Search for more literature for 4.6.1.18

Protein Variants

Protein Variants	Comment	Organism
A20P	thermodynamic and kinetic stability is similar to wild-type ribonuclease A. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus
A20P/S21P	thermodynamic and kinetic stability is similar to wild-type ribonuclease A. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus
F46Y	thermodynamic and kinetic stability of the mutant is greatly decreased. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus
K31A/R33S	thermodynamic and kinetic stability of the mutant is greatly decreased. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus
K31A/R33S/F46Y	thermodynamic and kinetic stability of the mutant is greatly decreased. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus
L35A	thermodynamic and kinetic stability of the mutant is greatly decreased. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus
L35A/F46Y	thermodynamic and kinetic stability of the mutant is greatly decreased. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus
L35S	thermodynamic and kinetic stability of the mutant is greatly decreased. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus
L35S/F46Y	thermodynamic and kinetic stability of the mutant is greatly decreased. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus
N34D	thermodynamic and kinetic stability is similar to wild-type ribonuclease A. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus
S21L	thermodynamic and kinetic stability is similar to wild-type ribonuclease A. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus
S21P	thermodynamic and kinetic stability is similar to wild-type ribonuclease A. Mutation has no significant effect on the native conformation and catalytic activity	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P61823	-	-

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Release 2023.1 (January 2023)