Prolyl Endopeptidase

spinqualitylabelsall models Prolyl endopeptidase of Sphingomonas capsulata at 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Prolyl endopeptidases (PEPs) are a class of serine proteases which cleave peptide bonds on the c-terminal side of internal proline residues.

FunctionFunction

PEPs are thought to have a role in the degradation of neuropeptides due to the high concentration of PEPs in the brain and the fact that PEPs have been shown to degrade several neuropeptides(vasopressin, β-endorphin, thyroliberin). The distribution of PEP in the brain has been found to be similar to that of certain receptors of neuropeptides which supports PEPs being involved in the degradation of neuropeptide transmitters.

Binding MechanismBinding Mechanism

Catalytic( and β-propeller domains(

Pharmaceutical PossibilitiesPharmaceutical Possibilities

Both human and microbial PEP have been the focus of research into their viability as therapeutic agents for several diseases. The ability of PEPs to cleave internal proline peptide bonds is of interest in the treatment of Celiac Disease which is caused by a reaction to gluten, a proline rich protein found in wheat and wheat subspecies. CITE BESEDIN PEPs have also been linked to several neurological disorders due to high activity in the brain and proposed role in the degradation of neuropeptides.

Celiac DiseaseCeliac Disease

Celiac Disease(CD) is a genetic disorder marked by diarrhea, fatigue, weight loss, and villous atrophy due to the consumption of gluten and other prolamins found in wheat and wheat subspecies. The symptoms of CD are due to an auto-immune inflammatory reaction that occurs in the small intestine due to prolamins. Prolamins are rich in proline residues and known to be resistant to many proteases