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Literature summary for 3.4.21.122 extracted from
- Functional analysis of potential cleavage sites in the MERS-coronavirus spike protein (2018), Sci. Rep., 8, 16597 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | O15393 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| MERS coronavirus S-protein + H2O | - |
Homo sapiens | ? | - |
? |  |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | pre-cleavage of the S-protein substrate at the S1/S2 motif (RSVR) is important although not essential for subsequent MERS-S activation by TMPRSS2. The S2' site (RSAR) is required for robust viral entry into all cell lines tested and the integrity of one of the two arginines is sufficient for efficient entry. Cleavage at S2' is carried out by proteases recognizing a single arginine, most likely TMPRSS2 and cathepsin L. Mutation of the proposed cathepsin L site does not impact viral entry and double mutation of S1/S2 and S2' site is compatible with cathepsin L- but not TMPRSS2-dependent host cell entry | Homo sapiens |
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Release 2023.1 (January 2023)
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