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

Year: 1988

Type: article

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.

Source: FEBS Letters

DOI: 10.1016/0014-5793(88)80502-7

Authors: Jørgen Olsen, Gillian M. Cowell, Elaine Kønigshøfer, E.Michael Danielsen, Jette Møller, Liselotte Laustsen, Ole C. Hansen, Karen G. Welinder, Jan Engberg, Walter Hunziker, Martin Spiesst, Hans Sjöström, Ove Norén

Institutions: University of Copenhagen, ETH Zurich

Language: English

Topic: Peptidase Inhibition and Analysis

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W2056675361

FWCI: 8.266

Cites: 59

Cited by: 246

Related to: 10