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Literature summary for 3.4.24.35 extracted from

  • Rasch, M.G.; Lund, I.K.; Illemann, M.; H?yer-Hansen, G.; Gardsvoll, H.
    Purification and characterization of recombinant full-length and protease domain of murine MMP-9 expressed in Drosophila S2 cells (2010), Protein Expr. Purif., 72, 87-94.
    View publication on PubMed
Search for more literature for 3.4.24.35

Activating Compound

Activating Compound Comment Organism Structure
4-aminophenylmercuric acetate activation of pro-MMP-9 constructs at pH 7.0 Mus musculus

Application

Application Comment Organism
drug development MMP-9 is an attractive target for therapeutic intervention studies in mouse models Mus musculus

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type full-length MMP-9 and of a mutant version lacking the O-glycosylated linker region and hemopexin domains in Drosophila melanogaster S2 cells using the Drosophila metallothionein promoter, the native MMP-9 signal peptide is utilized for secretion contained in the beginning of the sequences Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information generation of a mutant version lacking the O-glycosylated linker region and hemopexin domains and containing only the protease domain, residues 1-447 Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Mus musculus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Mus musculus
Zn2+ zinc metalloprotease Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
82000
-
 1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE Mus musculus
92000
-
 1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Gelatin + H2O Mus musculus
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant activated MMP-9 dimers by gelatin affnity chromatography Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
epidermis MMP-9 protein is localized at the leading-edge keratinocytes in front of the migrating epidermal layer Mus musculus
-
keratinocyte
-
 Mus musculus
-
macrophage located within the granulation tissue Mus musculus
-
neutrophil
-
 Mus musculus
-
skin
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gelatin + H2O
-
 Mus musculus ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 60000-65000, extracellular proteolytically active disulfide-linked MMP-9 dimers, SDS-PAGE Mus musculus
monomer 1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE Mus musculus
More MMP-9 is composed of the classical MMP domains including the pro-, catalytic, zinc-binding, and hemopexin domains. MMP-9 contains three fibronectin type II repeats facilitating its binding to collagen. An O-glycosylated linker region unique for MMP-9 connects the protease domain with the hemopexin domains Mus musculus

Synonyms

Synonyms Comment Organism
matrix metalloproteinase-9
-
 Mus musculus
MMP-9
-
 Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Mus musculus

General Information

General Information Comment Organism
physiological function MMP-9 soluble pro-enzyme is implicated in pathological events including cancer invasion. During skin wound healing, MMP-9 is expressed by the migrating leading-edge keratinocytes upon re-epithelialization of the wound Mus musculus