| Literature DB >> 2901990 |
J Olsen1, G M Cowell, E Kønigshøfer, E M Danielsen, J Møller, L Laustsen, O C Hansen, K G Welinder, J Engberg, W Hunziker.
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.Entities:
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Year: 1988 PMID： 2901990 DOI： 10.1016/0014-5793(88)80502-7
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124