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Literature summary for 3.1.31.1 extracted from

  • Tanaka, A.
    Fluorometric study of the acid-induced denaturation of Staphylococcal nuclease and its mutant forms (2004), Biosci. Biotechnol. Biochem., 68, 1293-1298.
    View publication on PubMed
Search for more literature for 3.1.31.1

Protein Variants

Protein Variants Comment Organism
A90S pH-value, at which the acid-denaturation is half completed is 4.19, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.0 for the mutant enzyme compared to 1.8 for wild-type enzyme Staphylococcus sp.
G79S pH-value, at which the acid-denaturation is half completed is 4.39, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.4 for the mutant enzyme compared to 1.8 for wild-type enzyme Staphylococcus sp.
G88V pH-value, at which the acid-denaturation is half completed is 3.57, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 3.0 for the mutant enzyme compared to 1.8 for wild-type enzyme Staphylococcus sp.
H124L pH-value, at which the acid-denaturation is half completed is 2.98, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 2.8 for the mutant enzyme compared to 1.8 for wild-type enzyme Staphylococcus sp.
L25A pH-value, at which the acid-denaturation is half completed is 4.15, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.2 for the mutant enzyme compared to 1.8 for wild-type enzyme Staphylococcus sp.
V66L pH-value, at which the acid-denaturation is half completed is 3.36, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 2.6 for the mutant enzyme compared to 1.8 for wild-type enzyme Staphylococcus sp.
V66L/G79S/G88V pH-value, at which the acid-denaturation is half completed is 3.67, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.1 for the mutant enzyme compared to 1.8 for wild-type enzyme Staphylococcus sp.
V66L/G88V pH-value, at which the acid-denaturation is half completed is 3.42, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.6 for the mutant enzyme compared to 1.8 for wild-type enzyme Staphylococcus sp.

Organism

Organism UniProt Comment Textmining
Staphylococcus sp.
-
-
-

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.15
-
 pH-value, at which the acid-denaturation is half completed in wild-type enzyme Staphylococcus sp.