Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.

G M Cowell; E Kønigshøfer; E M Danielsen; O C Hansen; J Engberg; W Hunziker; Jørgen Olsen; Jette Møller; Lotte Laustsen; K G Welinder

Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.

G M Cowell, E Kønigshøfer, E M Danielsen, O C Hansen, J Engberg, W Hunziker, Jørgen Olsen, Jette Møller, Lotte Laustsen, K G Welinder

196 Citations (Scopus)

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.

Original language	English
Journal	FEBS Letters
Volume	238
Issue number	2
Pages (from-to)	307-14
Number of pages	7
ISSN	0014-5793
Publication status	Published - 1988

Cite this

@article{e2bffe9099fa11dd86a6000ea68e967b,

title = "Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.",

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.",

author = "Cowell, {G M} and E K{\o}nigsh{\o}fer and Danielsen, {E M} and Hansen, {O C} and J Engberg and W Hunziker and J{\o}rgen Olsen and Jette M{\o}ller and Lotte Laustsen and Welinder, {K G}",

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",

year = "1988",

language = "English",

volume = "238",

pages = "307--14",

journal = "F E B S Letters",

issn = "0014-5793",

publisher = "JohnWiley & Sons Ltd",

number = "2",

}

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

SN - 0014-5793

VL - 238

SP - 307

EP - 314

JO - F E B S Letters

JF - F E B S Letters

IS - 2

ER -

Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.

Abstract

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