Prolyl Endopeptidase: Difference between revisions
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=== Binding Mechanism === | |||
=== Inhibition === | |||
Initial classification of prolyl endopeptidases as [http://en.wikipedia.org/wiki/Serine_protease serine proteases] was due to their inhibition by [http://en.wikipedia.org/wiki/Diisopropyl_fluorophosphate DFP]. | |||
Structural data for ''Myxococcus xanthus'' PEP in [X] shows that a bound inhibitor causes the β-propeller domain to become tightly associated with the catalytic domain and subsequently block the active site to inhibit catalysis. | |||
== Function == | == Function == | ||
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PEPs may also have a more general role in the degradation of peptides as PEP activity is found in most major organs and many other peptidases cannot cleave proline residues. | PEPs may also have a more general role in the degradation of peptides as PEP activity is found in most major organs and many other peptidases cannot cleave proline residues. | ||
== Pharmaceutical Possibilities == | == Pharmaceutical Possibilities == | ||
