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Literature summary for 3.4.24.3 extracted from
- Substrate recognition by the collagen-binding domain of Clostridium histolyticum class I collagenase (2001), J. Biol. Chem., 276, 8761-8770.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E414Q | mutant enzyme with a with a lower level of hydrolytic activity against insoluble collagen compared to wild-type enzyme | Hathewaya histolytica |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
MW of various C-terminal segments | Hathewaya histolytica |
| 114200 | - |
mutant enzyme E414Q, MALDI-TOF mass spectrometry | Hathewaya histolytica |
| 114200 | - |
wild-type enzyme, MALDI-TOF mass spectrometry | Hathewaya histolytica |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Hathewaya histolytica | - |
type I collagenase ColG | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| full-length type I collagenase and C-terminal fragments | Hathewaya histolytica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Collagen + H2O | a collagen-binding domain specifically recognizes the triple-helical conformation made by three chains in the collagenous region | Hathewaya histolytica | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ColG | - |
Hathewaya histolytica |
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Release 2023.1 (January 2023)
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