Merck, P6675-1KU, Prolidase from porcine kidney

General description
Prolidase is a cytosolic exopeptidase. It is a homodimeric enzyme which requires divalent cations like manganese as a cofactor in its active site for its function.
Application
Prolidase from porcine kidney has been used:
in the enzymatic hydrolysis of porcine milk for the recovery of L-glutamine from proteins and peptides
in the proteolysis of skim milk for the determination of ε-(γ-glutamyl)lysine and free aminoacids
to determine its effect on the activity of enterococcin A 2000

Prolidase has an important role in recycling of proline and collagen production. It is used to study mutations in the PEPD gene that cause prolidase deficiency. It is used to hydrolyze proteins with C-terminal proline or hydroxyproline residues. Prolidase, product P6675 from porcine kidney, has been used to hydrolyze peptide bonds from the amino terminus when studying enzymatic methylation of membrane proteins.
Biochem/physiol Actions
Rare mutation in prolidase gene causes deficiency leading to massive imidodipeptiduria, elevated proline-containing dipeptides in plasma, recurrent infections, mental retardation and skin lesions.
Prolidase is an enzyme that catalyzes the hydrolysis of the imide bond between an α-carboxyl group and proline or hydroxyproline. The protein forms a homodimer that hydrolyzes dipeptides or tripeptides with C-terminal proline or hydroxyproline residues.
Physical form
Supplied as a lyophilized powder containing Tris buffer salt and MnCl2.
Other Notes
One unit will hydrolyze 1.0 μmole of Gly-Pro per min at pH 8.0 at 40 °C.