Substrates for peptidase S01.256: chymopasin
Peptide and protein substrates that are thought to be physiologically relevant are indicated by P. Peptide and protein substrates that are thought to be pathologically relevant are indicated by D. Peptide and protein substrates that are not physiologically relevant are indicated by N. Synthetic substrates are indicated by S. Click on the symbol to show only physiological, non-physiological or synthetic substrates, or here to display all substrates. How cleavage sites have been identified are indicated by the following evidence codes: NT = N-terminal sequencing, MS = mass spectroscopy, MU = mutation, CS = consensus sequence, LC = liquid chromatography. To see all annotated cleavages for a protein substrate, click on the UniProt Accession.
| Substrate | Uniprot | Residue range | Cleavage Site | Cleavage type | Evidence | P4 | P3 | P2 | P1 | P1' | P2' | P3' | P4' | Reference | CutDB | MERNUM |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Bz-Arg-Val-Trp-NHPhNO2 | Bz-Arg-Val-Trp-NHPhNO2 | S | Bz | Arg | Val | Trp | NAN | - | - | - | Reseland et al., 1997 | |||||
| Bz-Lys-Val-Tyr-NHPhNO2 | Bz-Lys-Val-Tyr-NHPhNO2 | S | Bz | Lys | Val | Tyr | NAN | - | - | - | Reseland et al., 1997 | |||||
| D-Lys-Val-Phe-NHPhNO2 | D-Lys-Val-Phe-NHPhNO2 | S | - | Dly | Val | Phe | NAN | - | - | - | Reseland et al., 1997 | |||||
| D-Ser-Leu-Met-NHPhNO2 | D-Ser-Leu-Met-NHPhNO2 | S | - | Dse | Leu | Met | NAN | - | - | - | Reseland et al., 1997 | |||||
| Glutaryl-Ala-Ala-Pro-Leu-NHPhNO2 | Glutaryl-Ala-Ala-Pro-Leu-NHPhNO2 | S | Ala | Ala | Pro | Leu | NAN | - | - | - | Reseland et al., 1997 | |||||
| OMe-Suc-Arg-Pro-Tyr-NHPhNO2 | OMe-Suc-Arg-Pro-Tyr-NHPhNO2 | S | Ome | Arg | Pro | Tyr | NAN | - | - | - | Reseland et al., 1997 |
