Prolidase

Prolidase, also known as imidopeptidase or peptidase D, is a metalloprotease enzyme. It belongs to the M24 peptidase family. The primary role of prolidase is to catalyze the hydrolysis of dipeptides containing a proline residue at the C-terminal position. This means it breaks the peptide bond between two amino acids when the second amino acid has proline at its end. This activity is crucial for the breakdown of proteins rich in proline, such as collagen.

Prolidase is found in many organisms, including bacteria, plants, and mammals. In humans, prolidase is present in various tissues, with high concentrations found in the skin, liver, and kidneys. Its activity is important for processes like wound healing, collagen remodeling, and the metabolism of proline-containing peptides. A deficiency in prolidase activity leads to a rare autosomal recessive genetic disorder known as prolidase deficiency. This condition is characterized by skin abnormalities, recurrent infections, and intellectual disability. The enzyme requires a divalent metal ion, typically manganese or zinc, as a cofactor for its catalytic function.