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Literature summary for 3.4.21.66 extracted from

  • Behnke, U.; Ruttloff, H.; Kleine, R.
    Preparation and characterization of proteases from Thermoactinomyces vulgaris. V. Investigations on autolysis and thermostability of the purified protease (1982), Z. Allg. Mikrobiol., 22, 511-519.
    View publication on PubMed

General Stability

General Stability Organism
Autolysis and thereby inactivation at elevated temperature, at alkaline pH-values and in the absence of added substrate Thermoactinomyces vulgaris
Ca2+ stabilizes against both autolysis and thermal denaturation Thermoactinomyces vulgaris

Inhibitors

Inhibitors Comment Organism Structure
HgCl2
-
Thermoactinomyces vulgaris

Organism

Organism UniProt Comment Textmining
Thermoactinomyces vulgaris
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
Thermoactinomyces vulgaris hydrolyzed casein
-
?
N-Acetyl-L-Tyr ethyl ester + H2O
-
Thermoactinomyces vulgaris ?
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
denaturation above Thermoactinomyces vulgaris

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
autolysis and thereby inactivation at alkaline pH Thermoactinomyces vulgaris