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Literature summary for 3.1.31.1 extracted from

  • Wang, M.; Feng, Y.; Yao, H.; Wang, J.
    Importance of the C-terminal loop L137-S141 for the folding and folding stability of staphylococcal nuclease (2010), Biochemistry, 49, 4318-4326.
    View publication on PubMed
Search for more literature for 3.1.31.1

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)/pLysS Staphylococcus sp.

Protein Variants

Protein Variants Comment Organism
additional information generation by site-directed mutagenesis of C-terminal truncated SNases, i.e. SNase137, SNase139, SNase140, and SNase141 containing residues 1-137, 1-139, 1-140, and 1-141, respectively. The mutants show reduced activities compared to the wild-type enzyme. Determination of the secondary structures of the four SNase fragments, overview Staphylococcus sp.

Organism

Organism UniProt Comment Textmining
Staphylococcus sp.
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1270
-
 purified recombinant mutant SNase137, pH 7.4, 25°C Staphylococcus sp.
1319
-
 purified recombinant mutant SNase139, pH 7.4, 25°C Staphylococcus sp.
2018
-
 purified recombinant mutant SNase140, pH 7.4, 25°C Staphylococcus sp.
2298
-
 purified recombinant mutant SNase141, pH 7.4, 25°C Staphylococcus sp.
2553
-
 purified recombinant wild-type SNase, pH 7.4, 25°C Staphylococcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate is single-strand salmon sperm DNA Staphylococcus sp. ?
-
 ?

Synonyms

Synonyms Comment Organism
SNase
-
 Staphylococcus sp.
staphylococcal nuclease
-
 Staphylococcus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Staphylococcus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Staphylococcus sp.

General Information

General Information Comment Organism
additional information thermodynamic parameters derived from urea-induced unfolding of mutant SNase140 and mutant SNase141 in comparison with those of wild-type SNase and mutant SNase140 in the presence of calcium, backbone dynamics, detailed overview. Mutant SNase140 unfolds easily compared to mutant SNase141 and wild-type SNase Staphylococcus sp.