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

Olsen, J. and Cowell, G. M. and Konigshofer, E. and Danielsen, E. M. and Moller, J. and Laustsen, L. and Hansen, O. C. and Welinder, K. G. and Engberg, J. and Hunziker, W. and Spiess, Martin and Sjostrom, H. and Noren, O.. (1988) Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA. FEBS Letters, 238 (2). pp. 307-314.

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Official URL: http://edoc.unibas.ch/45486/

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Growth & Development > Biochemistry (Spiess)
UniBasel Contributors:Spiess, Martin
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Wiley
ISSN:0014-5793
e-ISSN:1873-3468
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:20 Nov 2017 10:14
Deposited On:20 Nov 2017 10:14

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