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Literature summary for 3.4.24.34 extracted from
- Pivotal molecular determinants of peptidic and collagen triple helicase activities reside in the S3 subsite of matrix metalloproteinase 8 (MMP-8): the role of hydrogen bonding potential of ASN188 and TYR189 and the connecting cis bond (2005), J. Biol. Chem., 280, 2370-2377.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E198A | mutant enzyme is not activated by 4-aminophenylmercuric acetate, no collagen cleavage activity | Homo sapiens |
| N188G | 25% decrease in collagen cleavage, 30% decrease in cleavage of (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-[3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-Ala-Arg-NH2 | Homo sapiens |
| N190L | unstable | Homo sapiens |
| Y189F | 88% of wild-type activity with (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-[3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-Ala-Arg-NH2. Activity against type I collagen dripps 3fold compared with wild-type enzyme | Homo sapiens |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 79000 | - |
x * 79000, recombinant mutant enzymes are purified in the proenzyme form and all display an apparent molecular mass of 79000 Da, SDS-PAGE | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | recombinant mutant enzymes are purified in the proenzyme form and all display an apparent molecular mass of 79000 Da, 4-aminophenylmercuric acetate-initiated autolytic processing to the fully activated form of the purified mutants, generation of the 59000 Da active enzyme after removal of the propeptide | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-[3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-Ala-Arg-NH2 + H2O | - |
Homo sapiens | ? | - |
? |  |
| Collagen + H2O | - |
Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 79000, recombinant mutant enzymes are purified in the proenzyme form and all display an apparent molecular mass of 79000 Da, SDS-PAGE | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MMP-8 | - |
Homo sapiens |
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