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Literature summary extracted from

  • Kleine, R.
    Properties of thermitase, a thermostable serine protease from Thermoactinomyces vulgaris (1982), Acta Biol. Med. Ger., 41, 89-102.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.4.21.66 The stability is significantly improved by 1 M acetate and chloride Thermoactinomyces vulgaris

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.66 extracellular
-
 Thermoactinomyces vulgaris
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.66 Thermoactinomyces vulgaris
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.66
-
 Thermoactinomyces vulgaris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.66 Collagen + H2O
-
 Thermoactinomyces vulgaris Hydrolyzed collagen
-
 ?
3.4.21.66 Elastin + H2O
-
 Thermoactinomyces vulgaris Hydrolyzed elastin
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.66 additional information
-
 the temperature optimum increases with incresing MW of substrate Thermoactinomyces vulgaris
3.4.21.66 60
-
 esterolysis Thermoactinomyces vulgaris
3.4.21.66 85
-
 proteinolysis Thermoactinomyces vulgaris

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.66 7.5 9.5
-
 Thermoactinomyces vulgaris

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.21.66 6 7.5 maximal stability Thermoactinomyces vulgaris