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Literature summary extracted from

  • Spencer, D.; Bertrand, G.M.; Stites, W.E.
    The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model (2013), Biophys. Chem., 180-181, 86-94.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.1.31.1 additional information generation of six single mutations were made in a highly stable triple mutant of nucleasemost nuclease, the mutants do not denature by a three-state mechanism, modeling, overview Staphylococcus aureus
3.1.31.1 P117G,/H124L/S128A site-directed mutagenesis, a highly stable triple mutant Staphylococcus aureus
3.1.31.1 V66F/P117G,/H124L/S128A site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared Staphylococcus aureus
3.1.31.1 V66G/P117G,/H124L/S128A site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared Staphylococcus aureus
3.1.31.1 V66N/P117G,/H124L/S128A site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared Staphylococcus aureus
3.1.31.1 V66Q/P117G,/H124L/S128A site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared Staphylococcus aureus
3.1.31.1 V66S/P117G,/H124L/S128A site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared Staphylococcus aureus
3.1.31.1 V66T/P117G,/H124L/S128A site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared Staphylococcus aureus
3.1.31.1 V66Y/P117G,/H124L/S128A site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
3.1.31.1 Staphylococcus aureus
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pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.31.1 5 10 recombinant mutant enzymes, stable, overview Staphylococcus aureus