Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

pepN - aminopeptidase

Escherichia coli CFT073

Onohara, Y. et al., Addlagatta, A. et al., Ito, K. et al., Contreras-Rodriguez, A. et al., Hatanaka, T. et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of pepN

The B. melitensis pepN gene was cloned, expressed in Escherichia coli and purified by affinity chromatography [1].
Characterization, cloning, sequencing, and expression of an aminopeptidase N from Streptomyces sp. TH-4 [2].

High impact information on pepN

Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site [3].
Aminopeptidase N from Escherichia coli is a major metalloprotease that participates in the controlled hydrolysis of peptides in the proteolytic pathway [3].
Crystal Structure of Aminopeptidase N (Proteobacteria Alanyl Aminopeptidase) from Escherichia coli and Conformational Change of Methionine 260 Involved in Substrate Recognition [4].
A recombinant form of aminopeptidase N (molecular weight 99 kDa) from Escherichia coli was crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitating agent [5].

Analytical, diagnostic and therapeutic context of pepN

Crystallization and preliminary X-ray characterization of aminopeptidase N from Escherichia coli [5].

References

Cloning, expression and characterization of immunogenic aminopeptidase N from Brucella melitensis. Contreras-Rodriguez, A., Seleem, M.N., Schurig, G.G., Sriranganathan, N., Boyle, S.M., Lopez-Merino, A. FEMS Immunol. Med. Microbiol. (2006) [Pubmed]
Characterization, cloning, sequencing, and expression of an aminopeptidase N from Streptomyces sp. TH-4. Hatanaka, T., Arima, J., Uraji, M., Uesugi, Y., Iwabuchi, M. Appl. Microbiol. Biotechnol. (2007) [Pubmed]
Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site. Addlagatta, A., Gay, L., Matthews, B.W. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
Crystal Structure of Aminopeptidase N (Proteobacteria Alanyl Aminopeptidase) from Escherichia coli and Conformational Change of Methionine 260 Involved in Substrate Recognition. Ito, K., Nakajima, Y., Onohara, Y., Takeo, M., Nakashima, K., Matsubara, F., Ito, T., Yoshimoto, T. J. Biol. Chem. (2006) [Pubmed]
Crystallization and preliminary X-ray characterization of aminopeptidase N from Escherichia coli. Onohara, Y., Nakajima, Y., Ito, K., Xu, Y., Nakashima, K., Ito, T., Yoshimoto, T. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg