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Literature summary for 3.4.21.75 extracted from
- The structure of the TGF-beta latency associated peptide region determines the ability of the proprotein convertase furin to cleave TGF-beta s (2007), J. Cell. Biochem., 103, 311-320.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| synthetic construct | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| chimeric transforming growth factor-beta1/beta2 + H2O | consists of the transforming growth factor-beta1 LAP region, the transforming growth factor-beta2 cleavage site and the transforming growth factor-beta2 mature peptide | synthetic construct | ? | - |
? |  |
| chimeric transforming growth factor-beta1/beta2 + H2O | efficiently cleaved | synthetic construct | ? | - |
? | |
| additional information | regular (short) form of transforming growth factor-beta2 and its spliced variant with an additional exon (long form) are insensitive to furin | synthetic construct | ? | - |
? | |
| additional information | transforming growth factor-beta2 and its spliced variant with an additional exon (long form) are insensitive to furin. Transforming growth factor-beta2 is only inefficiently cleaved as a consequence of the isoform specific characteristics of its latency-associated peptide region structures | synthetic construct | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| furin convertase | - |
synthetic construct |
| Proprotein convertase | - |
synthetic construct |
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Release 2023.1 (January 2023)
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