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Literature summary for 3.4.24.7 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

Inhibitors Comment Organism Structure
EDTA
-
Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
uterus
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Rattus norvegicus

pH Range

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