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Aminopeptidase is a generic term for enzymes that catalyze the hydrolysis of amino acids from the N-terminus of peptides or proteins. Most are metalloenzymes, requiring zinc, manganese, or similar ions for activity, though cysteine- and serine-dependent forms exist. Found throughout animal and plant tissues in cytosol, membranes, and organelles, aminopeptidases mediate key steps in protein digestion, maturation, cellular recycling of proteins, and participate in diverse processes from immunity to angiogenesis. Dysregulation or abnormal activity is linked to cancer, inflammation, hypertension, and infection. Aminopeptidase inhibitors have therapeutic potential, especially in oncology and cardiovascular medicine, but safety concerns arise due to the broad physiological roles of these enzymes.
Competitive inhibition of the active site by bestatin or similar small molecules; Chelation or replacement of essential metal ions inhibiting metalloaminopeptidase activity; Inhibition of substrate binding or turnover of peptides
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