Olsen J, Cowell G M, Kønigshøfer E, Danielsen E M, Møller J, Laustsen L, Hansen O C, Welinder K G, Engberg J, Hunziker W
Department of Biochemistry C, Panum Institute, University of Copenhagen, Denmark.
FEBS Lett. 1988 Oct 10;238(2):307-14. doi: 10.1016/0014-5793(88)80502-7.
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.
从一个cDNA克隆的序列推导出人肠氨肽酶N（EC 3.4.11.2）的完整一级结构（967个氨基酸）。氨肽酶N通过一个未切割的膜插入信号锚定在微绒毛膜上。位于催化结构域内的构成氨基酸250 - 555的结构域与大肠杆菌氨肽酶N具有非常明显的同源性，并含有锌离子配体。因此，这些残基是活性位点的一部分。然而，未发现锚定/连接肽结构域的同源性，这表明该分子的近膜和膜内部分在发育过程中已被添加/保留。据推测，这部分带有顶端定位信号。
