| Activity |
|---|
| Catalytic type | Serine |
| Peplist | Included in the Peplist with identifier PL00368 |
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.14 (Dipeptidyl-peptidase and tripeptidyl-peptidases) >> Peptidase 3.4.14.5
|
| Enzymology | BRENDA database |
| Proteolytic events | CutDB database (9 cleavages) |
| Activity status | human: active (Misumi & Ikehara, 2004)
mouse: active (Reimer et al., 2002)
|
| Physiology | Dipeptidyl-peptidase IV has numerous biological functions in eukaryotes, including involvement in T-cell activation, cell adhesion, digestion of proline containing peptides in the kidney and intestines, HIV infection and apoptosis, and regulation of tumorigenicity in certain melanoma cells (Pethiyagoda et al., 2001). Amongst the important activities is the destruction of the insulinotropic hormone, glucagon-like peptide 1 (GLP-1) (Holst & Deacon, 1998; Deacon & Holst, 2002). |
| Knockout | Fischer 344/CRJ rats harbor a G633R substitution in the gene that leads to retention and degradation of the mutant protein in the endoplasmic reticulum (Tsuji et al., 1992). The strain has been used as a knockout model to study involvement of the enzyme in metabolism of polypeptide hormones (Pederson et al., 1996) and tumor metastasis (Cheng et al., 1999). |
| Pharmaceutical relevance | Inhibition of DPPIV is a rational strategy to treat type II diabetes, in view of the sparing effect that inhibitors have on the glucagon-like peptide 1 (GLP-1) that is normally metabolised by this enzyme (Nagakura et al., 2001). Long-term inhibition was found to improve glucose tolerance in both normal and glucose-intolerant mice (Reimer et al., 2002). |
| Pathways |
KEGG | Protein digestion and absorption |
|
Other databases
| TREEFAM | http://www.treefam.org/family/TF313309 |
| Cleavage site specificity |
Explanations of how to interpret the
following cleavage site sequence logo and specificity matrix can be found here. |
|---|
| Cleavage pattern | p/h/g/P -/f/-/- (based on 35 cleavages) |
