Aminopeptidase Antikörper

Aminopeptidases are widely distributed in eukaryotes and prokaryotes. These enzymes catalyze the removal of amino acids from the N-termini of proteins. As a cell surface, zinc-dependent metalloprotease, Aminopeptidase A specifically cleaves amino-terminal acidic residues from peptide substrates such as Angiotensin II. Aminopeptidase B-L1 belongs to the M1 family and shares 49% identity with Aminopeptidase B. Aminopeptidase P is a member of the peptidase clan MG. It is a mammalian bradykinin-degrading, metal-dependant enzyme that is proline- specific; it cleaves the N-terminal amino acid where the second residue is proline. Aminopeptidase P2 belongs to the pita bread fold family of peptidase proteins that exists as a homotrimer that functions as a metalloprotease and plays a role in Bradykinin metabolism, as well as in inflammatory responses throughout the body. Aminopeptidase P3 belongs to the aminopeptidase family and uses manganese as a cofactor to catalyze the release of any proline-linked N-terminal amino acid, including those that exist in di- or tripeptides. The cytoplasm to vacuole targeting (Cvt) pathway is an autophagy-related trafficking pathway whose cargo proteins, aminopeptidase I and α-mannosidase, are selectively transported from the cytoplasm to the lysosome-like vacuoles in yeast.