Literature summary for 3.1.31.1 extracted from

Pais, T.M.; Lamosa, P.; Matzapetakis, M.; Turner, D.L.; Santos, H.
Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow beta-sheet motions (2012), Protein Sci., 21, 1126-1137.

Search for more literature for 3.1.31.1

Protein Variants

Protein Variants	Comment	Organism
P117G/H124L/S128A	site-directed mutagenesis	Staphylococcus aureus

General Stability

General Stability	Organism
correlation between the magnitude of protein stabilization and the restriction of fast backbone motions, mannosylglycerate restricts local motions in addition to the global motions of the protein. Unfolding/folding pathway remain undisturbed in the presence of mannosylglycerate but the solute shows a specific effect on the local motions of beta-sheet residues	Staphylococcus aureus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	P117G/H124L/S128A mutant enzyme thermodynamics, overview	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	-	-	-

Subunits

Subunits	Comment	Organism
More	solution structure of the hyperstable P117G/H124L/S128A mutant enzyme variant, overview	Staphylococcus aureus

Synonyms

Synonyms	Comment	Organism
SNase	-	Staphylococcus aureus
staphylococcal nuclease	-	Staphylococcus aureus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	different concentrations of mannosylglycerate or presence of urea at 0.25M show no correlation with changes in the thermodynamic stability of the P117G/H124L/S128A mutant enzyme	Staphylococcus aureus

General Information

General Information	Comment	Organism
additional information	mannosylglycerate preferentially affects specific structural elements of the P117G/H124L/S128A mutant enzyme, structure analysis, overview	Staphylococcus aureus

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Release 2023.1 (January 2023)