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Literature summary extracted from
- Purification, staphylolytic activity, and cleavage sites of alpha-lytic protease from Achromobacter lyticus (1997), J. Biochem., 122, 772-778.
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.12 | 19910 | - |
ion-spray mass spectrometry | Achromobacter lyticus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.12 | Achromobacter lyticus | - |
M497-1 | - |
| 3.4.21.12 | Achromobacter lyticus M497-1 | - |
M497-1 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.21.12 | - |
Achromobacter lyticus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.12 | additional information | - |
- |
Achromobacter lyticus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.12 | peptidoglycan + H2O | - |
Achromobacter lyticus | ? | - |
? |  |
| 3.4.21.12 | peptidoglycan + H2O | - |
Achromobacter lyticus M497-1 | ? | - |
? | |
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