Structural highlights
Function
PPCE_PIG Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A new inhibitor, containing a linked proline-piperidine structure, for the enzyme prolyl oligopeptidase (POP) has been synthesised and demonstrated to bind covalently with the enzyme at the active site. This provides evidence that covalent inhibitors of POP do not have to be limited to structures containing five-membered N-containing heterocyclic rings.
Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide.,Racys DT, Rea D, Fulop V, Wills M Bioorg Med Chem. 2010 Jul 1;18(13):4775-82. Epub 2010 May 31. PMID:20627594[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Racys DT, Rea D, Fulop V, Wills M. Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide. Bioorg Med Chem. 2010 Jul 1;18(13):4775-82. Epub 2010 May 31. PMID:20627594 doi:10.1016/j.bmc.2010.05.012
