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BRENDA support

Literature summary for 3.4.24.7 extracted from

  • Goldberg, G.I.; Wilhelm, S.M.; Kronberger, A.; Bauer, E.A.; Grant, G.A.; Eisen, A.Z.
    Human fibroblast collagenase. Complete primary structure and homology to an ancogene transformation-induced rat protein (1986), J. Biol. Chem., 261, 6600-6605.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
51929
-
x * 51929, the minor glycosylated enzyme form has a MW of 57000 Da, calculation from nucleotide sequence Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme is secreted in the form of a zymogen, proteolytic activation of procollagenase results in removal of 81 amino acid residues from the amino-terminal portion of the proenzyme Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
-
Homo sapiens
-

Subunits

Subunits Comment Organism
? x * 51929, the minor glycosylated enzyme form has a MW of 57000 Da, calculation from nucleotide sequence Homo sapiens