Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA |
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| Authors: | J Olsen G M Cowell E K?nigsh?fer E M Danielsen J M?ller L Laustsen O C Hansen K G Welinder J Engberg W Hunziker |
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| Institution: | Department of Biochemistry C, Panum Institute, University of Copenhagen, Denmark. |
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| Abstract: | 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. |
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