Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | FEBS Letters |
Volume | 238 |
Issue number | 2 |
Pages (from-to) | 307-14 |
Number of pages | 7 |
ISSN | 0014-5793 |
Publication status | Published - 1988 |
Bibliographical note
Keywords: Amino Acid Sequence; Aminopeptidases; Animals; Antigens, CD13; Base Sequence; Catalysis; Cloning, Molecular; Codon; DNA; Escherichia coli; Humans; Intestines; Molecular Sequence Data; Nucleic Acid Hybridization; Protein Biosynthesis; RNA, Messenger; Rabbits; Sequence Homology, Nucleic Acid; Swine
ID: 6586586