proline dipeptidase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: H2O + a dipeptide with proline at the C-terminal = L-proline + a standard alpha amino acid. [EC:3.4.13.9]

Proline dipeptidase activity is a catalytic activity that involves the hydrolysis of a peptide bond at the N-terminal end of a dipeptide, where the N-terminal amino acid residue is proline. This enzymatic activity is crucial for the breakdown of dietary proteins and the metabolism of peptides within the body. Proline dipeptidases are typically found in the gastrointestinal tract, where they contribute to the digestion of proteins. They also play a role in the breakdown of peptides in the liver and kidneys, and in the regulation of intracellular protein levels. The hydrolysis of proline-containing dipeptides by proline dipeptidases releases free proline, which is an essential amino acid for the synthesis of collagen and other proteins. Additionally, proline dipeptidases can contribute to the regulation of cellular signaling pathways by cleaving signaling peptides.'
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Proteins (1)

Compounds (2)