tripeptide aminopeptidase activity

Definition

Target type: molecularfunction

Catalysis of the hydrolysis of a single N-terminal amino acid residue from a tripeptide. [EC:3.4.11.4]

Tripeptide aminopeptidase activity is a molecular function associated with enzymes that specifically cleave the N-terminal amino acid from tripeptides. These enzymes belong to the peptidase family and play crucial roles in various biological processes. Tripeptide aminopeptidases typically exhibit a high degree of substrate specificity, preferentially recognizing tripeptides with specific amino acid residues at the N-terminus. The catalytic mechanism involves the hydrolysis of the peptide bond between the N-terminal amino acid and the adjacent residue, releasing a free amino acid and a dipeptide. This activity is essential for protein degradation, amino acid metabolism, and the regulation of cellular processes. Tripeptide aminopeptidases are involved in the breakdown of dietary proteins, the recycling of amino acids, and the activation or inactivation of peptides that act as signaling molecules. Their specific roles vary depending on the cellular context and the organism. For instance, some tripeptide aminopeptidases are involved in immune responses, while others play a role in development and differentiation. Understanding the molecular function of tripeptide aminopeptidases is crucial for comprehending complex biological processes and for developing potential therapeutic targets for various diseases.'
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Proteins (1)

Compounds (42)