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Literature summary for 3.4.24.28 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
Search for more literature for 3.4.24.28

Protein Variants

Protein Variants Comment Organism
G8C/N60C double mutation Geobacillus stearothermophilus

Inhibitors

Inhibitors Comment Organism Structure
guanidine hydrochloride competitive inhibitor Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Neutral protease
-
 Geobacillus stearothermophilus

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

Ki Value [mM]

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