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Literature summary for 3.4.21.85 extracted from
- Horseshoe Crab Coagulation Factor B. A unique serine protease zymogen activated by cleavage of an Ile-Ile bond (1993), J. Biol. Chem., 268, 2138-21388.
No PubMed abstract available
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 40570 | - |
x * 40570, calculated | Tachypleus tridentatus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Tachypleus tridentatus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | sequence contains a prepropeptide of 23 amino acids, that may be processed by both a signal peptidase and a processing protease. Cleavage sites of the zymogen for activation by limulus active factor C are an Arg-Ser and an Ile-Ile bond | Tachypleus tridentatus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 40570, calculated | Tachypleus tridentatus |
| More | mature enzyme is composed of an amino-terminal clip-like domain and a carboxyl-terminal serine protease domain homologous to that of human plasma prekallikrein | Tachypleus tridentatus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| factor B | - |
Tachypleus tridentatus |
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Release 2023.1 (January 2023)
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