TABLE 1.
Cleavage specificity of S. gordonii PepV
| Peptidea | % Cleavageb |
|---|---|
| Ala-↓-Ala | 100 |
| Ala-↓-Phe | 100 |
| Pro-↓-Phe | 100 |
| Leu-↓-Gly | 100 |
| Met-↓-Tyr | 100 |
| Gly-↓-Gly-↓-Ala | 75 |
| Gly-↓-Pro-Ala | 20 |
| Ala-↓-Phe-Pro | 20 |
| Ala-↓-Pro-Gly | 6 |
a
Cleavage sites are indicated by arrows. Cleavage sites for tripeptides were deduced from the appearance on HPLC of a dipeptide peak corresponding to the decrease in the tripeptide. No such dipeptide peaks were seen for Gly-Gly-Ala, indicating that both peptide bonds could be cleaved. The following peptides were not cleaved: Ala-His (carnosine), Ala-Pro, Gly-Pro, Ile-Pro, Leu- Pro, Lys-Pro, Ser-Pro, Gly-Gly, Gly-Pro-Arg-Pro (fibrin inhibitory peptide), and Trp-Ala-Gly- Gly-Asp-Ala-Ser-Gly-Glu (sleep-inducing peptide).
b
The percent cleavage is defined as (1 − area of residual peptide peak after digestion/area of peptide peak in undigested control) × 100.