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Literature summary for 3.4.24.34 extracted from

  • Knäuper, S.; Krämer, S.; Reinke, H.; Tschesche, H.
    Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms (1990), Eur. J. Biochem., 189, 295-300.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53000
-
x * 53000, human, deglycosylated enzyme, SDS-PAGE, under reducing conditions, x * 64000-65000, human, SDS-PAGE, x * 85000, human, latent enzyme, SDS-PAGE, under reducing conditions Homo sapiens
85000
-
x * 53000, human, deglycosylated enzyme, SDS-PAGE, under reducing conditions, x * 64000-65000, human, SDS-PAGE, x * 85000, human, latent enzyme, SDS-PAGE, under reducing conditions Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
as latent enzyme Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
leukocyte polymorphonuclear Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-(D)-Arg + H2O
-
Homo sapiens ?
-
?
Monomeric type I collagen + H2O from human Homo sapiens collagen type I fragment TCA + collagen type I fragment TCB
-
?
Monomeric type II collagen + H2O
-
Homo sapiens collagen type II fragment TCA + collagen type II fragment TCB
-
?
Monomeric type III collagen + H2O
-
Homo sapiens collagen type III fragment TCA + collagen type III fragmentTCB
-
?

Subunits

Subunits Comment Organism
? x * 53000, human, deglycosylated enzyme, SDS-PAGE, under reducing conditions, x * 64000-65000, human, SDS-PAGE, x * 85000, human, latent enzyme, SDS-PAGE, under reducing conditions Homo sapiens