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Literature summary for 3.4.24.19 extracted from

  • Kessler, E.; Adar, R.; Goldberg, B.; Niece, R.
    Partial purification and characterization of a procollagen C-proteinase from the culture medium of mouse fibroblasts (1986), Coll. Relat. Res., 6, 249-266.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Amines
-
Mus musculus
Blood serum
-
Mus musculus
DTT
-
Mus musculus
leupeptin not Mus musculus
metal chelators
-
Mus musculus
additional information not: inhibitors of serine Mus musculus
NEM
-
Mus musculus
pepstatin not Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
125000
-
mouse, gel filtration Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
culture medium of cultured mouse fibroblasts Mus musculus
-
tendon
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Procollagen type I + H2O cleavage occurs at the physiological site, i.e. at the specific Ala-Asp bond in the pro-alpha1(I) and pro-alpha2(I) chains, and at the specific Gly-Asp bond in the pro-alpha1(III) Mus musculus Type I pNcollagen + C-propeptides pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides ?
Procollagen type II + H2O
-
Mus musculus Type II pNcollagen + C-propeptides pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides ?
Procollagen type III + H2O
-
Mus musculus Type III pNcollagen + C-propeptides pNcollagen is an intermediate in the processing of procollagen to collagen containing the amino propeptides but not the carboxyl propeptides ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Mus musculus