Prolyl Endopeptidase
From Proteopedia
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| - | == Prolyl Endopeptidases == | ||
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<applet load='1yr2' size='300' frame='true' align='right' caption='Prolyl endopeptidase of Sphingomonas capsulata' /> | <applet load='1yr2' size='300' frame='true' align='right' caption='Prolyl endopeptidase of Sphingomonas capsulata' /> | ||
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| + | Prolyl endopeptidases (PEPs) are a class of serine proteases known to have a role in the degradation of neuropeptides and peptide hormones. PEPs are large enzymes (75kDa) that cleave after proline residues in the peptide chain. | ||
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| + | == Structure == | ||
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| + | == Function == | ||
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| + | === Binding Mechanism === | ||
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| + | === Inhibition === | ||
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| + | == Pharmaceutical Possibilities == | ||
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| + | === Celiac Disease === | ||
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| + | === Neurological Disorders === | ||
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| + | == References == | ||
Revision as of 19:37, 24 March 2010
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Prolyl endopeptidases (PEPs) are a class of serine proteases known to have a role in the degradation of neuropeptides and peptide hormones. PEPs are large enzymes (75kDa) that cleave after proline residues in the peptide chain.
Contents |
Structure
Function
Binding Mechanism
Inhibition
Pharmaceutical Possibilities
Celiac Disease
Neurological Disorders
References
Proteopedia Page Contributors and Editors (what is this?)
Stacey Shantz, Michal Harel, Alexander Berchansky, Joel L. Sussman, Andrea Gorrell, David Canner
