Prolyl endopeptidases |
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| Authors: | J Gass C Khosla |
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| Institution: | (1) Department of Chemical Engineering, Stanford University, Stanford, California 94305, USA;(2) Department of Chemistry, 380 Roth Way, Keck Chemistry Building, Stanford University, Stanford, California 94305, USA |
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| Abstract: | This review describes the structure and function of prolyl endopeptidase (PEP) enzymes and how they are being evaluated as
drug targets and therapeutic agents. The most well studied PEP family has a two-domain structure whose unique seven-blade
β-propeller domain works with the catalytic domain to hydrolyze the peptide bond on the carboxyl side of internal proline
residues of an oligopeptide substrate. Structural and functional studies on this protease family have elucidated the mechanism
for peptide entry between the two domains. Other structurally unrelated PEPs have been identified, but have not been studied
in detail. Human PEP has been evaluated as a pharmacological target for neurological diseases due to its high brain concentration
and ability to cleave neuropeptides in vitro. Recently, microbial PEPs have been studied as potential therapeutics for celiac sprue, an inflammatory disease of the small
intestine triggered by proline-rich gluten.
Received 6 July 2006; received after revision 17 August 2006; accepted 1 November 2006 |
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| Keywords: | Prolyl endopeptidase β -propeller neurological disorder celiac sprue gluten |
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