Aminopeptidases are enzymes that catalyze the cleavage of amino acids from the N-terminus (beginning), of proteins or peptides. They are found in many organisms; in the cell, they are found in many organelles, in the cytosol (internal cellular fluid), and as membrane proteins.

Feb 1, 1993 · Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein or peptide substrates. They are widely distributed throughout the animal and plant kingdoms and are found in many subcellular organelles, in cytoplasm, and as membrane components. Several aminopeptidases perform essential cellular functions.

Aminopeptidase N (APN, EC 3.4.11.2) is a widely studied peptidase, which is known under a variety of names, including aminopeptidase M, alanine aminopeptidase, arylamidase, and microsomal α‐aminoacyl‐peptide hydrolase.

Aminopeptidase is an integral membrane enzyme that cleaves aspartyl or glutamyl residues from peptides. It has been localized to cerebral microvessels and is involved in the degradation of CCK in the cortex and hippocampus. You might find these chapters and articles relevant to this topic.

By combining lysosomal proteomics with functional genomics, we identified PLBD1 (phospholipase B domain–containing 1), renamed LyLAP (lysosomal leucine aminopeptidase), as a top-ranking lysosomal hydrolase in cells that undergo high rates of endocytosis, specifically PDA and phagocytic immune cells.

5 days ago · Dysregulation of aminopeptidase activity has been linked to various diseases, including cancer, hypertension, and neurodegenerative disorders, highlighting their potential as therapeutic targets. Aminopeptidases are found across all domains of life, from bacteria to humans, with varying substrate specificities. Well-studied examples include ...

Aminopeptidases are enzymes that selectively hydrolyze an amino acid residue from the N-terminus of proteins and peptides. They are important for the proper functioning of prokaryotic and eukaryotic cells. The largest aminopeptidase group include enzymes containing metal ion(s) in their active centers. - MedChemexpress Biology Dictionary

Aminopeptidases (APs) are metalloenzymes that hydrolyze peptides and polypeptides by scission of the N-terminus amino acid and that also participate in the intracellular final digestion of proteins. APs play an important role in protein maturation, signal transduction, and cell-cycle control, among other processes.

Mar 28, 2025 · Combining lysosomal proteomics with functional genomic datasets, we identified lysosomal leucine aminopeptidase (LyLAP; formerly phospholipase B domain-containing 1) as the hydrolase most tightly associated with elevated endocytosis.

Aminopeptidase is a plasma membrane-bound enzyme present on macrophages as well as a variety of other cells. In human peripheral blood or bone marrow, the enzyme is reported to be present on monocytes and granulocytes but not on lymphocytes, basophils, or promyelocytes.