Literature summary for 3.1.31.1 extracted from

Ishii, T.; Murayama, Y.; Katano, A.; Maki, K.; Kuwajima, K.; Sano, M.
Probing force-induced unfolding intermediates of a single staphylococcal nuclease molecule and the effect of ligand binding (2008), Biochem. Biophys. Res. Commun., 375, 586-591.

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Protein Variants

Protein Variants	Comment	Organism
A1C/Q149C	SNase double mutant, N- and C-terminal residues replaced by cysteine, constructed from the plasmid (pMT7-SN) of wild-type SNase using the Kunkel method, can form disulfide bond	Staphylococcus sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
deoxythymidine 3',5'-diphosphate	in the presence of pdTp, unfolding forces increase drastically	Staphylococcus sp.

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	1 mM, unfolding forces in the presence of calcium ion are slightly increased	Staphylococcus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
DNA + H2O	Staphylococcus sp.	-	3'-deoxymononucleotides + dinucleotides	-	?

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus sp.	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
10 mM DTT added to expose sulfhydryl groups, and the solution passes through a short column of PD-10 to remove the reducing agent	Staphylococcus sp.

Renatured (Commentary)

Renatured (Comment)	Organism
atomic force microscopy, unfolding experiment: multiplicity of unfolding intermediates of SNase at the single-molecule level, mechanical unfolding pathways can be changed drastically under the acid-denatured condition (native conditions: 1 mM EGTA, pH 8.0, acid-denaturated condition: 1 mM EGTA, pH 2.5) or in the presence of ligands (Ca2+) and inhibitors (2'-deoxythymidine 3',5'-diphosphate)	Staphylococcus sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DNA + H2O	-	Staphylococcus sp.	3'-deoxymononucleotides + dinucleotides	-	?

Subunits

Subunits	Comment	Organism
monomer or dimer	small globular protein (149 amino acid residues), native protein: no disulfide bond, double mutant (A1C/Q149C): can form disulfide bond	Staphylococcus sp.

Synonyms

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

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Release 2023.1 (January 2023)