Prolyl oligopeptidase

Prolyl oligopeptidase (PO) is mapped to human chromosome 6q22. It comprises of a N-terminal β-propeller domain and C-terminal α/β hydrolase catalytic domain. PO is highly expressed in the neuronal cytoplasm and its expression increases with age.

Prolyl oligopeptidase is a cytosolic serine peptidase which cleaves peptide bonds at the C′ terminal side of prolines. It is only capable of processing peptides containing no more than 30 amino acids due to the unique β-propeller region that regulates access to the active site.

Prolyl oligopeptidase has been used in a study to assess the mechanism of lithium ion action. It has also been used in a study to investigate its distribution in human tissue and body fluids.

Prolyl oligopeptidase has been used in the prolyl oligopeptidase inhibitory activity assay in lyophilized protein hydrolysate samples and Schistosoma mansoni samples.

Prolyl oligopeptidase (PO) regulates physiological processes and is crucial for the generation of active hormone and peptide fragments from their precursors. It shows elevated levels in psychiatric disorders and Alzheimer′s patients. Altered levels of PO is observed in patients with bipolar disorder. High expression of PO may promote metastasis of malignant ovarian and colorectal tumors.

One unit will hydrolyze 1.0 picomole of Ala-Pro-aminomethylcoumarin per minute at pH 7.4 at 25 °C.

Supplied as a solution in 45 mM Tris-HCl, pH 8.0, 124 mM NaCl, 2.4 mM KCl, 10% glycerol, 3 mM DTT and variable amounts of imidazole.

N-terminal GST-tagged 81.6 kDa full-length protein