COMPLETE AMINO-ACID SEQUENCE OF HUMAN INTESTINAL AMINOPEPTIDASE-N AS DEDUCED FROM CLONED CDNA
COMPLETE AMINO-ACID SEQUENCE OF HUMAN INTESTINAL AMINOPEPTIDASE-N AS DEDUCED FROM CLONED CDNA
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DOI：
10.1016/0014-5793(88)80502-7
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发表时间：
1988-10-10
期刊：
影响因子：
3.5
通讯作者：
NOREN, O
中科院分区：
文献类型：
--
作者：
OLSEN, J;COWELL, GM;NOREN, O
从cDNA克隆的序列中推导出肠内人氨肽酶N（EC 3.4.11.2）的完整一级结构（967个氨基酸）。氨肽酶N通过膜插入的未切割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的结构域显示出与E非常明显的同源性。大肠杆菌氨基肽酶N和含有Zn 2+配体。因此，这些残基是活性位点的一部分。然而，未发现锚/连接肽结构域的同源性，表明在发育过程中添加/保留了分子的膜内和膜外部分。据推测，这部分携带顶端地址。
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 toE. coliaminopeptidase 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.