Family S15
Summary for family S15
| Family type peptidase | S15.001 - Xaa-Pro dipeptidyl-peptidase (Lactococcus lactis), MEROPS Accession MER0000443 (peptidase unit: 1-763) |
| Content of family | Peptidase family S15 contains Xaa-Pro dipeptidyl peptidase and its homologues. |
| History |
Identifier created: Biochem.J. 290:205-218 (1993)
|
| Catalytic type | Serine |
| Active site residues | S348 D468 H498 |
| Active site | The catalytic triad is in the order Ser348, His468, Asp498. |
| Activities and specificities | Xaa-Pro dipeptidyl-peptidase (S15.001) cleaves Xaa-Pro from the N-terminus of peptides provided that there is not a Pro in the P2 or P1" positions (Lloyd & Pritchard, 1991. It may also release Xaa-Ala and Xaa-Gly dipeptides, but more slowly than Xaa-Pro dipeptides (Khalid & Marth, 1990; Lloyd & Pritchard, 1991). |
| Inhibitors | DFP and PMSF are both inhibitors of Xaa-Pro dipeptidyl-peptidase. |
| Molecular structure | Xaa-Pro dipeptidyl-peptidase is homodimeric with a 2-fold symmetry axis (Rigolet et al., 2002). There are four distinct domains. The largest is an alpha/beta hydrolase fold which contains the catalytic triad. The shortest domain is responsible for substrate binding specificity and is also involved in dimerisation. The N-terminus is mainly responsible for the dimerisation (Chich, 2004). |
| Clan | SC |
| Basis of clan assignment | Predicted active site residues for members of this family and family S10 occur in the same order in the sequence: S, D, H. |
