Literature summary for 3.1.31.1 extracted from

Feng, Y.; Huang, S.; Zhang, W.; Zeng, Z.; Zou, X.; Zhong, L.; Peng, J.; Jing, G.
The effects of amino acid replacements of glycine 20 on conformational stability and catalysis of staphylococcal nuclease (2004), Biochimie, 86, 893-901.

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Protein Variants

Protein Variants	Comment	Organism
G20A	2% of wild-type activity. Km(Ca) is almost 20fold higher than the wild-type enzyme. Denaturation midpoint for the mutant enzyme is 1.5 M urea compared to 2.0 M urea for the wild-type enzyme	Staphylococcus sp.
G20I	0.21% of wild-type activity. Km(Ca) is almost 50fold higher than the wild-type enzyme. Denaturation midpoint for mutant enzyme is 0.82 M urea compared to 2.0 M urea for the wild-type enzyme	Staphylococcus sp.
G20V	0.45% of wild-type activity. Km(Ca) is almost 20fold higher than the wild-type enzyme. Denaturation midpoint for the mutynt enzyme is 1.1 M urea compared to 2.0 M urea for the wild-type enzyme	Staphylococcus sp.

General Stability

General Stability	Organism
denaturation midpoint for urea is 1.5 M for mutant G20A, 1.1 M urea for mutant G20V, 0.82 Murea or mutant G20I and 2.0 M for wild-type enzyme	Staphylococcus sp.

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	hydrolysis of DNA and RNA is completely dependent on Ca2+, KM for wild-type enzyme is 0.113 mM	Staphylococcus sp.

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus sp.	-	-	-

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)