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Literature summary extracted from

  • Duerrschmidt, P.; Mansfeld, J.; Ulbrich-Hofmann, R.
    Differentiation between conformational and autoproteolytic stability of the neutral protease from Bacillus stearothermophilus containing an engineered disulfide bond (2001), Eur. J. Biochem., 268, 3612-3618.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.28 G8C/N60C double mutation Geobacillus stearothermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.28 guanidine hydrochloride competitive inhibitor Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.28 Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.28 wild-type and mutant enzymes Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.28 N-(3-[2-furyl]acryloyl)-Gly-Leu amide + H2O
-
Geobacillus stearothermophilus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.28 Neutral protease
-
Geobacillus stearothermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.28 60
-
activity toward N-(3-[2-furyl]acryloyl)-Gly-Leu amide is 4 times higher than at 25°C Geobacillus stearothermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.24.28 25 65
-
Geobacillus stearothermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.24.28 92.5
-
G8C/N60C double mutation extremely thermostable, half-life 35.9 min Geobacillus stearothermophilus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.24.28 1000
-
guanidine hydrochloride pH 7.5, 25°C Geobacillus stearothermophilus