Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase
IPR001930
Definition
This group of metallopeptidases belong to the MEROPS peptidase family M1 (clan MA(E)), the type example being aminopeptidase N from Homo sapiens (Human). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA. Membrane alanine aminopeptidase ([ec:3.4.11.2]) is part of the HEXXH+E group; it consists entirely of aminopeptidases, spread across a wide variety of species PMID:7674922. Functional studies show that CD13/APN catalyses the removal of single amino acids from the amino terminus of small peptides and probably plays a role in their final digestion; one family member (leukotriene-A4 hydrolase) is known to hydrolyse the epoxide leukotriene-A4 to form an inflammatory mediator PMID:7674922. This hydrolase has been shown to have aminopeptidase activity PMID:2244921, and the zinc ligands of the M1 family were identified by site-directed mutagenesis on this enzyme PMID:7674922 CD13 participates in trimming peptides bound to MHC class II molecules PMID:8691132 and cleaves MIP-1 chemokine, which alters target cell specificity from basophils to eosinophils PMID:8627182. CD13 acts as a receptor for specific strains of RNA viruses (coronaviruses) which cause a relatively large percentage of upper respiratory tract infections.
12 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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