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Literature summary for 3.4.24.17 extracted from
- pH stability of the stromelysin-1 catalytic domain and its mechanism of interaction with a glyoxal inhibitor (2011), Biochim. Biophys. Acta, 1814, 1394-1403.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | catalytic domain (residues 83-247) are used in this study | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| (betaR)-beta-[[[(1S)-1-[[[(1S)-2-methoxy-1-phenylethyl]amino]carbonyl]-2,2-dimethylpropyl]amino]carbonyl]-2-methyl-[1,1'-biphenyl]-4-hexanoic acid | UK-370106-COOH, potent inhibitor | Escherichia coli |  |
| UK-370106-COCHO | glyoxal inhibitor, created by conversion of the carboxylate group of UK-370106-COOH to a glyoxal group. At pH 5.5-6.5 the glyoxal inhibitor is a potent inhibitor of stromelysin-1 | Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.395 | - |
acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 | pH 6.0, 25°C, catalytic domain (residues 83-247) | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purified from Escherichia coli | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 + H2O | - |
Escherichia coli | ? | - |
? | |
| Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys (Dnp) + H2O | - |
Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| stromelysin-1 | catalytic domain (residues 83-247) are used in this study | Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
assay at | Escherichia coli |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4.5 | - |
at pHs 4.5 and 10.0 irreversible denaturation is biphasic | Escherichia coli |
| 5 | - |
at pHs 5.0 and 9.0 there is exponential irreversible denaturation with half lives of 38 and 68 min, respectively | Escherichia coli |
| 6.8 | 8.4 | stable for at least 16 h at pHs 6.0-8.4 | Escherichia coli |
| 9 | - |
at pHs 5.0 and 9.0 there is exponential irreversible denaturation with half lives of 38 and 68 min, respectively | Escherichia coli |
| 10 | - |
at pHs 4.5 and 10.0 irreversible denaturation is biphasic | Escherichia coli |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.001 | - |
UK-370106-COCHO | pH 5.5-6.5, 25°C | Escherichia coli | |
| 0.0107 | - |
UK-370106-COCHO | pH 7.56, 37°C | Escherichia coli | |
| 0.0188 | - |
UK-370106-COCHO | pH 7.56, 25°C | Escherichia coli | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.6 | - |
acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 | pH 6.0, 25°C, catalytic domain (residues 83-247) | Escherichia coli | |
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