Pz-Peptidase is an enzyme of high affinity to collagen oligopeptides.

Proteos biotech´s Pz-Peptidase is considered essential for the degradation of collagen in collaboration with collagenolytic enzymes. The properties of Pz-Peptidase are: (1) They are metallooligoproteases; (2) They have a Zn2+-chelating HEXXH motif; (3) They have no significant amino acid sequence similarity to C. histolyticum collagenases ColG and ColH; (4) They show hydrolyzing activity toward oligopeptides but not toward protein substrates.

We produce pure recombinant Pz-Peptidase using affinity chromatography. Our enzyme proceed from Bacillus licheniformis (PWD) and are produced in E. coli. Our Pz-Peptidase has been adapted to the laboratory conditions and suitable for cell culture studies.

Pz-Peptidases can also hydrolyze neuropeptides, such as bradykinin and neurotensin (Fig).At the same peptide bond, they have been found to be inert towards Pz-PLGPR and FALGPA (Monnet et al. 1994; Tobiassen et al. 1997; Christensson et al. 2002).

Pz-Peptidase has also been implicated in regulating cleavage of the amyloid-β-peptide, which, when aberrantly processed, has been linked to Alzheimer’s disease pathogenesis (Yamin et al. 1999). Therefore, bacterial Pz-Peptidases could be applied to the development of new therapeutic drugs that simulate the reaction mechanism in the cleavage of the amyloid-β-peptide

Pz-Peptidase is active and present the following physical and chemical parameters: • Molecular Weight (MW): 76.95 KDa • Isoelectric Point (pI): 5.16