Final answer:
Matrix metalloproteinases (MMPs) are a class of metalloproteinase that cleave several types of endogenous peptides and proteins, particularly in the extracellular matrix, and are involved in processes like wound healing and tissue remodeling.
Step-by-step explanation:
The question asks about a metalloproteinase that cleaves and inactivates a specific endogenous peptide. Metalloproteinases are a group of proteases, which are enzymes that break down proteins into smaller peptides or amino acids. Matrix metalloproteinases (MMPs) are a well-studied group of these enzymes that play a key role in the breakdown of extracellular matrix components during physiological processes such as tissue remodeling, wound healing, and embryonic development.
While the question does not specify which endogenous peptide is being inactivated, MMPs can cleave several kinds of peptides and proteins in the extracellular matrix, including but not limited to collagen, fibrin, and fibronectin. Knight example is when MMPs degrade collagen, they thereby play a significant part in wound healing and can also activate or release growth factors or morphogens through specific cleavages.
Additionally, proteases like aminopeptidases and carboxypeptidases also cleave peptides, with aminopeptidases acting on the amino terminal end and carboxypeptidases on the carboxy terminal end. The precise function and substrate specificity can vary significantly among different classes of proteases.