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Literature summary extracted from
- Identification of structural determinants controlling human and mouse stromelysin-3 proteolytic activities (1995), J. Biol. Chem., 270, 22866-22872.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.24.B3 | pharmacology | enzyme form with the specific residue A235 is an attractive target for the development of specific inhibitors for use in prevention of cancer progression | Homo sapiens |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.24.B3 | expression of truncated mutant lacking the N-terminal prodomain in Escherichia coli BL21(DE3), and the C-terminal part of the hemopexin-like domain, expression of wild-type enzyme in MFC7 cells | Mus musculus |
| 3.4.24.B3 | expression of truncated mutant lacking the N-terminal prodomain, the C-terminal part of the hemopexin-like domain, and mutant A235P in Escherichia coli BL21(DE3) | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.24.B3 | A235P | site-directed mutagenesis, alters substrate specificity, mutant processed and truncated enzyme additionally cleaves casein, laminin, and type IV collagen, Ala 235 is typical for the enzyme and is located immediately after the Met-turn, which forms a catalytic basis for the zinc ion | Homo sapiens |
| 3.4.24.B3 | P235A | site-directed mutagenesis, truncated mutant with this introduces point mutation shows reduced enzyme activity against laminin and collgen IV | Mus musculus |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.B3 | Zn2+ | metalloprotease, Zn2+ binding site is part of the catalytic centre | Mus musculus |  |
| 3.4.24.B3 | Zn2+ | zinc binding region including the motif HEXXHXXGXXH and the conserved methionine residue of the Met-turn ALMX, Ala 235 is typical for the enzyme and is located immediately after the Met-turn, which forms a catalytic basis for the zinc ion | Homo sapiens | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.B3 | 21000 | - |
x * 21000, recombinant processed and truncated form, SDS-PAGE | Mus musculus |
| 3.4.24.B3 | 22000 | - |
x * 22000, recombinant processed and truncated form, SDS-PAGE | Homo sapiens |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.B3 | protein + H2O | Mus musculus | enzyme is involved in both physiological and pathological tissue remodeling processes, including those associated with cancer progression | peptides | - |
? | |
| 3.4.24.B3 | protein + H2O | Homo sapiens | enzyme is involved in both physiological and pathological tissue remodeling processes, including those associated with cancer progression | peptides | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.24.B3 | Homo sapiens | - |
- |
- |
| 3.4.24.B3 | Mus musculus | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.24.B3 | proteolytic modification | formation of a processed and truncated mature form of MW 21 kDa | Mus musculus |
| 3.4.24.B3 | proteolytic modification | formation of a processed and truncated mature form of MW 22 kDa | Homo sapiens |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 3.4.24.B3 | mutant enzyme are solubilized and refolded from inclusion bodies after expression in Escherichia coli | Homo sapiens |
| 3.4.24.B3 | recombinant truncated enzyme is solubilized and refolded from inclusion bodies after expression in Escherichia coli | Mus musculus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.B3 | 20 | - |
recombinant processed and truncated enzyme, substrate beta-casein | Mus musculus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.B3 | casein + H2O | only recombinant processed enzyme lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus | Mus musculus | ? | - |
? | |
| 3.4.24.B3 | casein + H2O | only recombinant processed enzyme mutant A235P lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus | Homo sapiens | ? | - |
? | |
| 3.4.24.B3 | collagen type IV + H2O | only recombinant processed enzyme lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus | Mus musculus | ? | - |
? | |
| 3.4.24.B3 | collagen type IV + H2O | only recombinant processed enzyme mutant A235P lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus | Homo sapiens | ? | - |
? | |
| 3.4.24.B3 | Laminin + H2O | only recombinant processed enzyme lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus | Mus musculus | ? | - |
? | |
| 3.4.24.B3 | Laminin + H2O | only recombinant processed enzyme mutant A235P lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus | Homo sapiens | ? | - |
? | |
| 3.4.24.B3 | protein + H2O | - |
Mus musculus | peptides | - |
? | |
| 3.4.24.B3 | protein + H2O | - |
Homo sapiens | peptides | - |
? | |
| 3.4.24.B3 | protein + H2O | enzyme is involved in both physiological and pathological tissue remodeling processes, including those associated with cancer progression | Mus musculus | peptides | - |
? | |
| 3.4.24.B3 | protein + H2O | enzyme is involved in both physiological and pathological tissue remodeling processes, including those associated with cancer progression | Homo sapiens | peptides | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.24.B3 | ? | x * 21000, recombinant processed and truncated form, SDS-PAGE | Mus musculus |
| 3.4.24.B3 | ? | x * 22000, recombinant processed and truncated form, SDS-PAGE | Homo sapiens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.24.B3 | M10.007 | Merops-ID | Mus musculus |
| 3.4.24.B3 | M10.007 | Merops-ID | Homo sapiens |
| 3.4.24.B3 | matrix metalloproteinase-11 | - |
Mus musculus |
| 3.4.24.B3 | matrix metalloproteinase-11 | - |
Homo sapiens |
| 3.4.24.B3 | matrixin | - |
Mus musculus |
| 3.4.24.B3 | matrixin | - |
Homo sapiens |
| 3.4.24.B3 | MMP-11 | - |
Mus musculus |
| 3.4.24.B3 | MMP-11 | - |
Homo sapiens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.B3 | 37 | - |
assay at | Mus musculus |
| 3.4.24.B3 | 37 | - |
assay at | Homo sapiens |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.B3 | 7.5 | - |
assay at | Mus musculus |
| 3.4.24.B3 | 7.5 | - |
assay at | Homo sapiens |
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