TABLE 4.
Substrate specificity of the purified PepN enzyme from S. thermophilus A
| Substrates | Relative activity (%) | Substrate | Relative activity (%) | Hydrolyzed substratesa | Nonhydrolyzed substrates |
|---|---|---|---|---|---|
| Lys-AMC | 100 | Gly-Arg-AMC | <1 | Lys-▴Tyr | Glu-Lys |
| Leu-AMC | 93 | ||||
| Arg-AMC | 80 | Pro-Lys-AMC | <1 | Leu-▴Leu | Lys-Pro |
| Met-AMC | 28 | Pro-Phe-Arg-AMC | 0 | Leu-▴Arg | Leu-Pro |
| Ala-AMC | 20 | Leu-▴Tyr | Arg-Pro | ||
| Phe-AMC | 12 | bz-Phe-Val-Arg-AMC | 0 | Leu-▵Gly | |
| Tyr-AMC | 7 | suc-Ala-Phe-Lys-AMC | 0 | Arg-Pro-Pro | |
| Ser-AMC | 3 | Met-▴Leu | |||
| Val-AMC | 1 | Tyr-▴Leu | Tyr-Pro-Leu-Gly | ||
| Pro-AMC | 0 | ||||
| Gln-AMC | 0 | Leu-▴Leu-▴Leu | Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg | ||
| Glu-AMC | 0 | ||||
| Gly-AMC | 0 | Ala-▴Leu-▴Ala-▵Gly | |||
| Tyr-▴Gly-Gly-Phe-Met |
a
Solid black arrows indicate bonds cut by PepN. White arrows indicate slower hydrolysis.