Structural Basis for the Unusual Specificity of Escherichia coli Aminopeptidase N
Author:
Affiliation:
1. Institute of Molecular Biology, Howard Hughes Medical Institute, and Department of Physics, 1229 University of Oregon, Eugene, Oregon 97403-1229
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi7022333
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3. Purification, Characterization, Gene Cloning, Sequencing, and Overexpression of Aminopeptidase N from Streptococcus thermophilus A
4. PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress
5. PepN, the Major Suc-LLVY-AMC-hydrolyzing Enzyme inEscherichia coli, Displays Functional Similarity with Downstream Processing Enzymes in Archaea and Eukarya
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