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.

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.

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.

Rare mutation in prolidase gene causes deficiency leading to massive imidodipeptiduria, elevated proline-containing dipeptides in plasma, recurrent infections, mental retardation and skin lesions.

One unit will hydrolyze 1.0 μmole of Gly-Pro per min at pH 8.0 at 40 °C.

Supplied as a lyophilized powder containing Tris buffer salt and MnCl₂.