Crystal Structure of Aminopeptidase N (Proteobacteria Alanyl Aminopeptidase) from Escherichia coli and Conformational Change of Methionine 260 Involved in Substrate Recognition-Reference-Cited by-同舟云学术

Crystal Structure of Aminopeptidase N (Proteobacteria Alanyl Aminopeptidase) from Escherichia coli and Conformational Change of Methionine 260 Involved in Substrate Recognition

Published:2006-11 Issue:44 Volume:281 Page:33664-33676
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Ito Kiyoshi,Nakajima Yoshitaka,Onohara Yuko,Takeo Masahide,Nakashima Kanako,Matsubara Futoshi,Ito Takashi,Yoshimoto Tadashi

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress

2. Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV

3. Human aminopeptidase N is a receptor for human coronavirus 229E

4. Bacillus thuringiensisCry1Aa toxin-binding region ofBombyx moriaminopeptidase N

5. Aminopeptidase N isoforms from the midgut ofBombyx moriandPlutella xylostella- their classification and the factors that determine their binding specificity toBacillus thuringiensisCry1A toxin

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