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

FEBS Letters

Spiesst, Martin¹  Cowell, Gillian M.⁴  Laustsen, Liselotte⁴  Engberg, Jan³  Sjöström, Hans⁴  Danielsen, E.Michael⁴  Olsen, Jørgen⁴  Welinder, Karen G.²  Kønigshøfer, Elaine⁴  Hunziker, Walter¹  Møller, Jette⁴  Hansen, Ole C.⁵  Norén, Ove⁴ 

[1] Laboratorium für Biochemie II der Eidgenössigen Technischen Hochshule, ETH-Zentrum, CH-8092 Zürich, Switzerland;Institute of Biochemical Genetics, University of Copenhagen, Øster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark;Department of Biochemistry B, The Plenum Institute, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark;Department of Biochemistry C, The Panum Institute, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark;Protein Laboratory, The Panum Institute, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark

关键词: Aminopeptidase N;    cDNA cloning;    Amino acid sequence;    Active site;    Sorting signal;    (Caco 2 cell);   

DOI  :  10.1016/0014-5793(88)80502-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown