Prolyl Endopeptidase

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Prolyl endopeptidase of Sphingomonas capsulata

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

StructureStructure

β-Propeller Domainβ-Propeller Domain

Catalytic DomainCatalytic Domain

Domain InterfaceDomain Interface

FunctionFunction

PEPs are thought to have a role in the degredation 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).

Binding MechanismBinding Mechanism

InhibitionInhibition

Pharmaceutical PossibilitiesPharmaceutical Possibilities

Celiac DiseaseCeliac Disease

Neurological DisordersNeurological Disorders

ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Andrea Gorrell, Stacey Shantz, David Canner, Michal Harel, Alexander Berchansky, Joel L. Sussman