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Literature summary extracted from

  • Jeffrey, J.J.; Gross, J.
    Collagenase from rat uterus. Isolation and partial characterization (1970), Biochemistry, 9, 268-273.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.7 EDTA
-
 Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.7 Ca2+ required Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.7 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.7 uterus
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.7 Collagen + H2O below 30°C the enzyme catalyzes a small number of cleavages in the native collagen molecule with no loss in tertiary structure. Fragments of 75, 67, and 62% of the molecular length from the A end are formed. At 37°C and neutral pH, the enzyme degrades native collagen fibrils or molecules to peptides most of which are dialyzable Rattus norvegicus ?
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.24.7 90
-
 10 min, inactivation Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.7 7.5
-
-
 Rattus norvegicus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.24.7 5.8 9 pH 5.8: about 30% of maximal activity, pH 9.0: about 45% of maximal activity Rattus norvegicus