Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase (IPR001930)

Short name: Peptidase_M1

Overlapping homologous superfamilies

Family relationships


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: 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 catalyzes 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.

GO terms

Biological Process

GO:0006508 proteolysis

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.