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Literature summary for 3.4.24.B3 extracted from

  • Murphy, G.; Segain, J.P.; O'Shea, M.; Cockett, M.; Ioannou, C.; Lefebvre, O.; Chambon, P.; Basset, P.
    The 28-kDa N-terminal domain of mouse stromelysin-3 has the general properties of a weak metalloproteinase (1993), J. Biol. Chem., 268, 15435-15441.
    View publication on PubMed
Search for more literature for 3.4.24.B3

Cloned(Commentary)

Cloned (Comment) Organism
expression of an inactive enzyme in Escherichia coli BL21(DE3), expression of a functional enzyme in NSO mouse myeloma cell line Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline complete inhibition Mus musculus
EDTA complete inhibition Mus musculus
matrix metalloproteinase inhibitor TIMP-1 complete inhibition, human Mus musculus
additional information no inhibition by phosphoramidon and L-3-caroxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane, i.e. E-64 Mus musculus
phenylmethylsulfonyl fluoride slight inhibition Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
 x * 28000, recombinant active N-terminal domain, SDS-PAGE, x * 58000, inactive recombinant enzyme expressed in Escherichia coli, SDS-PAGE Mus musculus
58000
-
 x * 28000, recombinant active N-terminal domain, SDS-PAGE, x * 58000, inactive recombinant enzyme expressed in Escherichia coli, SDS-PAGE Mus musculus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification recombinant protein from mouse myeloma cells is cleaved and loses its propeptide and the majority of its C-terminal domain, recombinant enzyme can be cleaved by trypsin to a 51 kDa stil latent enzyme form Mus musculus

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli and NSO mouse myeloma cells Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
21
-
 purified recombinant latently active enzyme form Mus musculus
99
-
 purifed recombinant active enzyme form Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
aggrecan + H2O 28 kDa N-terminal domain, cartilage proteoglycan encapsulated in polyacrylamide beads Mus musculus ?
-
 ?
carboxymethylated transferrin + H2O 28 kDa N-terminal domain Mus musculus ?
-
 ?
casein + H2O 28 kDa N-terminal domain Mus musculus ?
-
 ?
collagen type IV + H2O only unfolded collagen, 28 kDa N-terminal domain Mus musculus ?
-
 ?
Fibronectin + H2O 28 kDa N-terminal domain Mus musculus ?
-
 ?
Gelatin + H2O 28 kDa N-terminal domain, low activity Mus musculus ?
-
 ?
Laminin + H2O 28 kDa N-terminal domain Mus musculus ?
-
 ?
additional information enzyme can activate the activity of trypsin-activated interstitial collagenase, no activation of prostromelysin-1, progelatinase A, progelatinase B, no activity with collagen type I Mus musculus ?
-
 ?
protein + H2O
-
 Mus musculus peptides
-
 ?

Subunits

Subunits Comment Organism
? x * 28000, recombinant active N-terminal domain, SDS-PAGE, x * 58000, inactive recombinant enzyme expressed in Escherichia coli, SDS-PAGE Mus musculus

Synonyms

Synonyms Comment Organism
M10.007 Merops-ID Mus musculus
matrix metalloproteinase-11
-
 Mus musculus
MMP-11
-
 Mus musculus

Temperature Optimum [°C]

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