Proline Specific Endopeptidase, isolated from Flavobacterium sp. (1,2), specifically cleaves peptide bonds on the carboxy side of proline residues. This enzyme is very close, in the properties, to post-proline cleaving enzyme discovered by Walter (3-5). The substrates have been found to have the general structure Y-Pro-X, where Y is a peptide or N-protected amino acid and X may be an amino acid, peptide, amide or ester. Much slower hydrolysis is observed when the substrate is Y-Ala-X (5).
Proline specific endopeptidase is useful for the determination of amino acid sequences of peptides and proteins containing proline residues. Proline specific endopeptidases may be useful in cancer, neurology and diabetes research . Prolyl endopeptidase (PEP) may be used as a drug target for neuropsychiatric diseases such as stress disorder, depression, and schizophrenia.
Molecular Weight:78kD
Activity:≥5 units/mg solid
Aminopeptidase:≤ 0.1%
Trypsin:≤ 0.1%
Optimum pH:7.0
Optimum Temp:40°C
Isoelectric Point:9.1
Km:1.25mM (Z-Gly-Pro-pNA)
Inhibitors:DFP, Z-Gly-Pro-CH2Cl2
Unit Definition:One unit of endopeptidase produces one micromole of p-nitroaniline per minute from Z-Gly-Pro-pNA at 30 Deg C at pH 7.0
Storage and Stability:Lyophilized powder may be stored at 4°C. Stable for 12 months at 4°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
