Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.
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Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA. / Cowell, G M; Kønigshøfer, E; Danielsen, E M; Hansen, O C; Engberg, J; Hunziker, W; Olsen, Jørgen; Møller, Jette; Laustsen, Lotte; Welinder, K G.
I: FEBS Letters, Bind 238, Nr. 2, 1988, s. 307-14.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.
AU - Cowell, G M
AU - Kønigshøfer, E
AU - Danielsen, E M
AU - Hansen, O C
AU - Engberg, J
AU - Hunziker, W
AU - Olsen, Jørgen
AU - Møller, Jette
AU - Laustsen, Lotte
AU - Welinder, K G
N1 - 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
PY - 1988
Y1 - 1988
N2 - 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.
AB - 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.
M3 - Journal article
C2 - 2901990
VL - 238
SP - 307
EP - 314
JO - F E B S Letters
JF - F E B S Letters
SN - 0014-5793
IS - 2
ER -
ID: 6586586