Literature summary for 3.1.31.1 extracted from

Nguyen, D.M.; Leila Reynald, R.; Gittis, A.G.; Lattman, E.E.
X-ray and thermodynamic studies of staphylococcal nuclease variants I92E and I92K: insights into polarity of the protein interior (2004), J. Mol. Biol., 341, 565-574.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals of the I92E and I92K variant proteins are obtained at 4°C using the hanging-drop vapor-diffusion method	Staphylococcus sp.

Protein Variants

Protein Variants	Comment	Organism
I92E	wild-type enzyme exhibits a broad range of pH-independence from pH 4.5 to pH 9, mutant enzyme exhibits pronounced pH-dependence with a maximal stability at pH 4.9	Staphylococcus sp.
I92K	wild-type enzyme exhibits a broad range of pH-independence from pH 4.5 to pH 9.0, mutant enzyme exhibits pronounced pH-dependence with a maximal stability at pH 9.8	Staphylococcus sp.

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus sp.	-	-	-

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
4.5	9	25°C, wild-type enzyme is stable in the range	Staphylococcus sp.
4.8	-	25°C, maximal stability of mutant enzyme I92E	Staphylococcus sp.
9.8	-	25°C, maximal stability of mutant enzyme I92K	Staphylococcus sp.

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Release 2023.1 (January 2023)