Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA
- 10 October 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 238 (2) , 307-314
- https://doi.org/10.1016/0014-5793(88)80502-7
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.Keywords
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