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Literature summary for 3.4.21.64 extracted from
- Long-range structural changes in proteinase K triggered by calcium ion removal (1989), Nature, 337, 481-484.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| X-ray crystal structure at 1.5 A resolution shows that it has 2 binding sites for Ca2+ | Parengyodontium album |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Calcium | X-ray studies show that it has 2 binding sites for Ca2+, Ca2+ is not directly involved in the catalytic mechanism and is 16.6 A away from the alpha-carbon atoms of the catalytic triad Asp39-His69-Ser224, the activity of the enzyme towards the synthetic substrate succinyl-Ala-Ala-Ala 4-nitroanilide drops slowly to about 20% of its original value when it is depleted of Ca2+ | Parengyodontium album |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Parengyodontium album | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O | - |
Parengyodontium album | ? | - |
? | |
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