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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Olsen J,Cowell GM,Kønigshøfer E,Danielsen EM,Møller J,Laustsen L,Hansen OC,Welinder KG,Engberg J,Hunziker Wdoi
10.1016/0014-5793(88)80502-7subject
Has Abstract,Author List Incompletepub_date
1988-10-10 00:00:00pages
307-14issue
2eissn
0014-5793issn
1873-3468journal_volume
238pub_type
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