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Literature summary extracted from

  • K๖ditz, J.; Ulbrich-Hofmann, R.; Arnold, U.
    Probing the unfolding region of ribonuclease A by site-directed mutagenesis (2004), Eur. J. Biochem., 271, 4147-4156.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.18 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
4.6.1.18 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
4.6.1.18 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
4.6.1.18 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
4.6.1.18 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
4.6.1.18 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
4.6.1.18 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
4.6.1.18 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
4.6.1.18 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
4.6.1.18 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
4.6.1.18 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
4.6.1.18 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

EC Number Organism UniProt Comment Textmining
4.6.1.18 Bos taurus P61823
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