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    FEBS Lett. 1988 Oct 10;238(2):307-14.

    Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.

    Olsen J, Cowell GM, Kønigshøfer E, Danielsen EM, Møller J, Laustsen L, Hansen OC, Welinder KG, Engberg J, Hunziker W, et al.

    Department of Biochemistry C, Panum Institute, University of Copenhagen, Denmark.

    The complete primary structure (967 amino acids) of an intestinal human aminopeptidase N (EC 3.4.11.2) was deduced from the sequence of a cDNA clone. Aminopeptidase N is anchored to the microvillar membrane via an uncleaved signal for membrane insertion. A domain constituting amino acid 250-555 positioned within the catalytic domain shows very clear homology to E. coli aminopeptidase N and contains Zn2+ ligands. Therefore these residues are part of the active site. However, no homology of the anchor/junctional peptide domain is found suggesting that the juxta- and intra-membraneous parts of the molecule have been added/preserved during development. It is speculated that this part carries the apical address.

    PMID: 2901990 [PubMed - indexed for MEDLINE]

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