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Literature summary for 3.4.24.35 extracted from
- Matrix metalloproteinase-9 activity detected in body fluids is the result of two different enzyme forms (2012), J. Biochem., 151, 493-499.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | enzyme MMP-9 is released in the inactive form as proenzyme and can be secreted in physical association with its specific tissue inhibitor (TIMP-1) as proMMP-9/TIMP-1 complex or as TIMP-1 free protein. Activation of MMP-9 requires a complex network of mechanisms involving other matrix metalloproteases | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| tissue inhibitor of metalloproteinases 1 | TIMP-1, the 65 kDa enzyme form lacking both the N- and C-terminal domains cannot be inhibited by TIMP-1 in contrast to the mature 82 kDa enzyme form | Homo sapiens |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 65000 | - |
x * 65000, active matured, truncated enzyme form lacking both the N- and C-terminal domains, SDS-PAGE, x * 82000, activated mature enzyme, SDS-PAGE | Homo sapiens |
| 65000 | 82000 | major circulating MMP-9 enzyme forms: 92 kDa proMMP-9, and active 82 kDa and 65 kDa enzyme forms | Homo sapiens |
| 82000 | - |
x * 65000, active matured, truncated enzyme form lacking both the N- and C-terminal domains, SDS-PAGE, x * 82000, activated mature enzyme, SDS-PAGE | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Gelatin + H2O | Homo sapiens | - |
? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P14780 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | enzyme MMP-9 is released in the inactive form as proenzyme as proMMP-9/TIMP-1 complex or as TIMP-1 free protein. Activation of MMP-9 requires a complex network of mechanisms involving other matrix metalloproteases. In vitro activation of enzyme matrix metalloproteinase-9 with MMP-3, EC 3.4.24.17, shows the presence of two different forms: an 82 kDa, N-terminal truncated form, and a 65 kDa, N- and C-terminal truncated form. 4-Aminophenylmercuric acetate activation induces an autoproteolytic activation causing the removal of the propeptide followed by a further breakage and subsequent formation of a N- and C-truncated form of 67 kDa | Homo sapiens |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme from serum samples by concanavalin-A and gelatin afffinity chromatography, and ultrafiltration | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| blood serum | - |
Homo sapiens | - |
| additional information | enzyme MMP-9 is released in the inactive form as proenzyme and can be secreted in physical association with its specific tissue inhibitor (TIMP-1) by monocyte/macrophage cells as proMMP-9/TIMP-1 complex or as TIMP-1 free protein by tertiary granules of neutrophil cells | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Gelatin + H2O | - |
Homo sapiens | ? | - |
? | |
| additional information | 4-aminophenylmercuric acetate activation induces an autoproteolytic activation of the enzyme zymogen causing the removal of the propeptide followed by a further breakage and subsequent formation of a N- and C-truncated form of 67 kDa | Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 65000, active matured, truncated enzyme form lacking both the N- and C-terminal domains, SDS-PAGE, x * 82000, activated mature enzyme, SDS-PAGE | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| gelatinase B | - |
Homo sapiens |
| matrix metalloproteinase-9 | - |
Homo sapiens |
| MMP-9 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | a truncated 65 kDa enzyme lacks the haemopexin domain required for the high-affinity binding of the tissue inhibitor TIMP-1, and can be evaluated by activity assay in the presence of tissue inhibitor of metalloproteinases 1, TIMP-1 | Homo sapiens |
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