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Literature summary for 3.4.24.28 extracted from

  • Duerrschmidt, P.; Mansfeld, J.; Ulbrich-Hofmann, R.
    Refolding of the non-specific neutral protease from Bacillus stearothermophilus proceeds via an autoproteolytically sensitive intermediate (2010), Biophys. Chem., 147, 66-73.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
G8C/N60C thermostable variant of the non-specific neutral protease Geobacillus stearothermophilus

General Stability

General Stability Organism
native wild type and G8C/N60C enzymes are stable toward autoproteolysis and keep their structural integrity for several weeks Geobacillus stearothermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 5 mM Ca2+ stabilizes the enzyme Geobacillus stearothermophilus
Zn2+ Zn2+ ions, although essential cofactors and exhibiting extremely high affinity, are without effect on the stability Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
protease activity can be significantly regained if the completely unfolded enzyme is transferred from 8 M guanidine-HCl into native-like conditions (0.4 M guanidine-HCl) by dilution with buffer Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-aminobenzoyl-Ala-Gly-Leu-Ala-4-nitrobenzylamide + H2O
-
Geobacillus stearothermophilus ?
-
?
casein + H2O
-
Geobacillus stearothermophilus ?
-
?

Synonyms

Synonyms Comment Organism
non-specific neutral protease
-
Geobacillus stearothermophilus