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Literature summary for 3.4.21.4 extracted from

  • De, D.; Chakraborty, P.D.; Bhattacharyya, D.
    Regulation of trypsin activity by peptide fraction of an aqueous extract of human placenta used as wound healer (2010), J. Cell. Physiol., 226, 2033-2040.
    View publication on PubMed

General Stability

General Stability Organism
a fibronectin type III-like peptide from aqueous extract of human placenta, used as a licensed drug for wound healing, tightly complexes the enzyme and protects it against autodigestion. Trypsin retains 40% of activity at constant level between 20 and 26 days in presence of the extract against complete inactivation in its absence. The peptide-trypsin complex is dissociated in presence of high concentration of substrates Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates, plays an important role in trypsin stabilization Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information trypsin shows protease and esterase activities Homo sapiens ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
protease activity assay at Homo sapiens
7.8
-
esterase activity assay at Homo sapiens
8.8
-
autodigestion assay at Homo sapiens

General Information

General Information Comment Organism
additional information a fibronectin type III-like peptide from aqueous extract of human placenta, used as a licensed drug for wound healing, tightly complexes the enzyme and regulates its activity, near-irreversible binding, modeling, overview Homo sapiens